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Mechanisms of cooperativity and allosteric regulation in proteins

  • M. F. Perutz (a1)


AUosteric proteins control and coordinate chemical events in the living cell. When Monod conceived that idea he said that he had discovered the second secret of life. The first was the structure of DNA. The theory as published by Monod et al. (1963) was concerned chiefly with cooperativity and feedback inhibition of enzymes, such as the inhibition of threonine deaminase, the first enzyme in the pathway of the synthesis of isoleucine, by isoleucine, and its activation by valine. Two years later the theory was formalized by Monod et al. (1965).



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Abelson, P. H., (1954). Amino acid biosynthesis in Escherichia coli: isotopic competition with 14C glucose. J. biol. Chem. 206, 335343.
Almassy, R. J., Janson, C. A., Hamlin, R., Xuong, N.-H. & Eisenberg, D. (1986). Novel subunit-subunit interactions in the structure of glutamine synthetase. Nature 323. 304309.
Amit, A. G., Mariuzza, R. A., Phillips, S. E. V. & Poljak, R. J. (1986). Three-dimensional structure of an antigen-antibody complex at 2·8 Å resolution. Science 233. 747753.
Antonini, E. & Brunori, M. (1971). Hemoglobin and Myoglobin and their Reactions with Oxygen, pp. 241, 394. Amsterdam: North Holland.
Angel, W.-L., Karplus, M., Poyart, C. & Burseaux, E. (1988). Analysis of proton release in oxygen binding by haemoglobin: implications for the cooperative mechanism. Biochemistry 27. 12851301.
Armstrong, W. H. & Lippard, S. J. (1984). Reversible protonation of the oxo bridge in a haemerythrin model compound. J. Am. Chem. Soc. 106, 46324633.
Armstrong, W. H., Spool, A., Papaefthymiou, G. C., Frankel, R. B. & Lippard, S. J. (1984). Assembly and characterisation of an accurate model for the diiron center in hemerythrin. J. Am. Chem. Soc. 106, 36533667.
Arnone, A. (1972). X-ray diffraction study of binding of 2, 3-diphosphoglycerate to human deoxyhaemoglobin. Nature 237. 146149.
Arrowsmith, C. H., Carey, J., Treat-Clemons, L. & Jardetzky, O. (1989). NMR assignments for the amino-terminal residues of trp repressor and their role in DNA binding. Biochemistry 28. 38753885.
Baldwin, J. M. (1975). Structure and function of haemoglobin. Progr. Biophys. molec. Biol. 29, 225320.
Baldwin, J. M. & Chothia, C. (1979). Haemoglobin: the structural changes related to ligand binding and its allosteric mechanism. J. molec. Biol. 129, 183191.
Barford, D. & Johnson, L. N. (1989). The allosteric transition of glycogen phosphorylase. Nature (in the Press).
Bass, S., Sugiono, P., Arvidson, D. N., Gunsalus, R. P. & Youderian, P. (1987). RNA specificity determinants of E. coli tryptophan repressor binding. Genes & Development 1, 565572.
Bennett, W. S. & Steitz, T. A. (1978). Glucose-induced conformational change in yeast hexokinase. Proc. natn. Acad. Sci. U.S.A. 75, 48484852.
Berger, S. A. & Evans, P. R. (1989). Active site mutants altering the cooperativity of E. coli phosphofructokinase. (In preparation.)
Blackburn, M. N. & Schachman, H. K. (1977). Allosteric regulation of aspartate transcarbamylase. Effect of active site ligands on the reactivity of sulfydryl groups of the regulatory subunits. Biochemistry 16. 50845090.
Blangy, D., Buc, H. & Monod, J. (1968). Kinetics of the allosteric interactions of phosphofructokinase from Escherichia coli. J. molec. Biol. 31, 1335.
Bloomer, A. C. & Butler, P. J. G. (1986). Tobacco mosaic virus: structure and assembly. In The Plant Viruses (ed. van Regenmortel, M. B. V. and Fraenkel-Conrat, H.). Plenum.
Bloomer, A. C., Champness, J. N., Bricogne, G., Staden, R. & Klug, A. (1978). Protein disk of tobacco mosaic virus at 2·8 Å resolution showing interactions within and between the subunits. Nature 276. 362368.
Bolognesi, M., Cannillo, E., Ascenzi, P., Giacometti, G. M., Merli, A. & Brunori, M. (1982). Reactivity of ferric Aplysia and sperm whale myoglobins towards imidazole: X-ray and binding study. J. molec. Biol. 158, 305315.
Bonaventura, C, Sullivan, B., Bonaventura, J. & Bourne, S. (1974). CO binding by hemocyanins of Limulus polyphemus, Busycon carica and Callinectes sapidus. Biochemistry 13. 47844789.
Briehl, R. W. (1963). The relation between the oxygen equilibrium and aggregation of subunits in lamprey hemoglobin. J. biol. Chem. 238, 23612366.
Brown, J. M., Powers, L., Kinkaid, B., Larrobee, J. A. & Spiro, T. G. (1980). Hemocyanin active site characterization and resonance Raman spectroscopy. J. Am. Chem. Soc. 102, 42104216.
Brunori, M., Kuiper, H. A. & Zolla, L. (1982). Ligand binding and stereochemical effects in hemocyanins. EMBO J. 1, 329331.
Bunn, H. F. & Forget, G. B. (1985). Hemoglobin, Molecular and Clinical Aspects. Philadelphia: W. B. Saunders.
Butler, P. J. G. & Durham, A. C. H. (1977). Tobacco mosaic virus protein aggregation and the virus assembly. Adv. Prot. Chem. 31, 187251.
Butler, P. J. G. & Klug, A. (1978). The assembly of a virus. Sci. Am. 239, 5259.
Calhoun, D. B., Vanderkooi, J. M., Woodrow, G. V. III & Englander, S. W. (1983). Penetration of dioxygen into proteins studied by quenching of phosphorescence and fluorescence. Biochemistry 22. 15261532.
Carey, J. (1988). Gel retardation at low pH resolves trp repressor-DNA complexes for quantitative study. Proc. natn. Acad. Sci. U.S.A. 85, 975979.
Carey, J. (1989). trp Repressor arms contribute binding energy without occupying unique locations on DNA. J. biol. Chem. 264, 19411945.
Carmichael, V. E., Dutton, P. J., Fyles, T. M., James, T. D., Swan, J. A. & Zojaji, M. (1989). Biomimetic ion transport: a functional model of a unimolecular ion channel. J. Am. Chem. Soc. III, 767769.
Caspar, D. (1963). Assembly and stability of the tobacco mosaic virus particle. Adv. Prot. Chem. 18, 37121.
Cash, D. J. & Hess, G. P. (1980). Molecular mechanism of acetylcholine-controlled ion translocation across cell membranes. Proc. natn. Acad. Sci. U.S.A. 77, 842846.
Changeux, J. P. (1961). The feedback mechanism of biosynthetic L-threonine deaminase by L-isoleucine. Cold Spring Harb. Symp. quant. Biol. 26, 313318.
Changeux, J. P., Gerhardt, J. C. & Schachman, H. K. (1968). Allosteric interaction in aspartate transcarbamylase. 1. Binding of specific ligands to the native enzyme and its isolated subunits. Biochemistry 7. 531538.
Changeux, J. P., Giraudat, J. & Dennis, M. (1987). The nicotinic acid acetylcholine receptor: molecular architecture of a ligand-regulated ion channel. Trends pharmac. Sci. 8, 450465.
Changeux, J. P. & Rubin, M. M. (1968). Allosteric interactions in aspartate transcarbamylase. III. Interpretation of experimental data in terms of the model of Monod, Wyman & Changeux. Biochemistry 7. 553560.
Cheng, X. & Schoenborn, (1989). Private communication.
Chothia, C. & Lesk, A. M. (1985). Helix movements in proteins. Trends in Biochem. Sci. 10, 116118.
Chu, A. H., Turner, B. W. & Ackers, G. K. (1984). Effects of protons on the oxygenlinked subassembly in human hemoglobin. Biochemistry 23. 604617.
Cohen, G. & Jacob, F. (1959). Sur la répression de la synthèse des enzymes intervenants dans la formation du tryptophane chez Escherichia coli. C. r. hebd. séanc. Acad. Sci., Paris 248. 34903492.
Connelly, P. R., Gill, S. J., Miller, K. I., Zhou, G. & van Holde, K. E. (1989). Identical linkage and cooperativity of oxygen and carbon monoxide binding to Octopus dofleini hemocyanin. Biochemistry 28. 18351843.
Crick, F. H. C. & Orgel, L. E. (1964). The theory of interallelic complementation. J. molec. Biol. 8, 161165.
Crothers, D. M. & Metzger, H. (1972). The influence of polyvalency on the binding properties of antibodies. Immunochemistry 9. 341357.
Dalvit, C. & Wright, P. E. (1987). Assignment of resonances in the 1H nuclear magnetic resonance spectrum of the carbonmonoxide complex of sperm whale myoglobin by phase-sensitive two-dimensional techniques. J. molec. Biol. 194, 313327.
Derewenda, Z., Dodson, G., Emsley, P., Harris, D., Nagai, K., Perutz, M. F. & Renaud, J.-P. (1989). The stereochemistry of CO binding to normal human adult and Cowtown hemoglobins. J. molec. Biol. (in the Press).
Dickerson, R. E. & Geis, I. (1983). Haemoglobin: Structure, Function, Evolution, Pathology. Kenlo Park: Benjamin/Cummings.
Di Gabriele, A. D., Sanderson, M. R. & Steitz, T. A. (1989). Crystal lattice packing is important in determining the bend of a DNA dodecamer containing an adenine tract. Proc. natn. Acad. Sci. U.S.A. 86, 18161920.
Dohi, D., Sugita, Y. & Yoneyama, Y. (1973). The self-association and oxygen equilibrium of hemoglobin from the lamprey Entosphenus japonicus. J. biol. Chem. 248, 23542363.
Eisenberg, D., Almassy, R. J., Janson, C. A., Chapman, M. S., Shuh, S. W., Cascio, D. & Smith, W. W. (1987). Some evolutionary relationships of the primary biological catalysts glutamine synthetase and RuBisCo. Cold Spring Harb. Symp. quant. Biol 52. 483490.
Eisenstein, E., Markby, D. W. & Schachman, H. K. (1989). Changes in stability and allosteric properties of aspartate transcarbamyolase resulting from amino acid substitutions in the zinc-binding domain of the regulatory chains. Proc. natn. Acad. Sci. U.S.A. 86, 30943098.
Elam, W. T., Stern, E. A., McCallum, J. D. & Sanders-Loehr, J. (1983). An X-ray absorption study of the binuclear iron center in deoxyhemerythrin. J. Am. Chem. Soc. 105, 19191923.
Elber, R. & Karplus, M. (1989). Molecular dynamics simulations of myoglobin. (To be published.)
Ellerton, H. D., Ellerton, N. F. & Robinson, H. A. (1983). Hemocyanin – a current perspective. Progr. Biophys. Molec. Biol. 41, 143248.
Englander, S. W. & Kallenbach, N. R. (1984). Hydrogen exchange and structural dynamics of proteins and nucleic acids. Q. Rev. Biophys. 16, 521565.
Evans, D. R., Styliani, C. P.-L. & Lipscomb, W. N. (1975). Isolation and properties of a species produced by the partial dissociation of aspartate transcarbamylase from Escherichia coli. J. biol. Chem. 250 (10), 35713583.
Evans, P. R. & Hudson, P. J. (1979). Structure and control of phosphofructokinase from Bacillus stearothermophilus. Nature 279. 500504.
Evans, P. R., Farrants, G. W. & Lawrence, M. C. (1986). Crystallographic structure of allosterically inhibited phosphofructokinase at 7 Å resolution. J. molec. Biol. 191, 713720.
Fermi, G. & Perutz, M. F. (1981). Atlas of Molecular Structures in Biology: Haemoglobin & Myoglobin. Oxford: Clarendon Press.
Fersht, A. R., Leatherbarrow, R. J. & Wells, T. N. C. (1986). Structure and activity of the tyrosyl-tRNA synthetase: the hydrogen bond in catalysis and specificity. Phil. Trans. R. Soc. Lond. A317, 305320.
Fincham, J. R. S. & Day, P. R. (1963). Fungal Genetics. Oxford: Blackwell Scientific Publications.
Fletterick, R. J. & Madsen, N. B. (1980). The structures and related functions of phosphorylase a. A. Rev. Biochem. 49, 3161.
Fletterick, R. J. & Sprang, S. R. (1982). Glycogen phosphorylase structures and function. Acc. Chem. Res. 15, 361369.
Foote, J. & Schachman, H. K. (1985). Homotropic effects in aspartate transcarbamylase: What happens when the enzyme binds a single molecule of the bisubstrate analogue N-phosphonacetyl-L-aspartate? J. molec. Biol 186. 175184.
Frederick, C. A., Grable, J., Melia, M., Samudzi, C, Jen-Jacobson, L., Wang, B. C., Greene, P., Boyer, H. W. & Rosenberg, J. M. (1984). Kinked DNA in crystalline complex with Eco RI endonuclease. Nature 309. 327331.
Frey, J. G., Eisenberg, D. & Eiserling, F. A. (1975). Glutamine synthetase forms three- and seven-stranded cables. Proc. natn. Acad. Sci. U.S.A. 72, 34023406.
Gaykema, W. P. J., Hol, W. G. J., Vereijken, J. M., Soeter, N. M., Bak, H. J. & Beintema, J. J. (1984). 3·2 Å structure of the copper-containing, oxygen-carrying protein Panulirus interruptus haemocyanin. Nature 309. 2329.
Gelin, R. G., Lee, A. W.-M. & Karplus, M. (1983). Hemoglobin tertiary structural change on ligand binding. Its role in the cooperative mechanism. J. molec. Biol. 171, 480559.
Gerhardt, J. C. & Pardee, A. B. (1962). The enzymology of control by feedback inhibition. J. biol. Chem. 237, 891896.
Gerhardt, J. C. & Schachman, H. K. (1968). Allosteric interactions in aspartate transcarbamylase II. Evidence for different conformational states of the protein in the presence and absence of specific ligands. Biochemistry 7. 538552.
Gibbons, I., Ritchey, J. M. & Schachman, H. K. (1976). Concerted allosteric transitions in hybrids of aspartate transcarbamyìase containing different arrangements of active and inactive sites. Biochemistry 15. 13241330.
Gibbons, I., Yang, Y. R. & Schachman, H. K. (1974). Cooperative interactions in aspartate transcarbamylase. I. Hybrids composed of native and chemically inactivated catalytic chains. Proc. natn. Acad. Sci. U.S.A. 71, 44524456.
Gill, S. J., Di Cera, E., Doyle, M. L. & Robert, C. H. (1988). New twists on an old story: hemoglobin. Trends biochem. Sci. 13, 465467.
Giraudat, J., Dennis, M., Heitmann, T., Haumont, P. T., Lederer, F. & Changeux, J. P. (1987). Structure of the high-affinity binding sites for non-competitive blockers of the acetylcholine receptor: [3H]chlorpromazine labels homologous residues in the β and δ chains. Biochemistry 26. 24102418.
Goldsmith, E., Sprang, S. & Fletterick, R. J. (1982). Structure of maltoheptaose by difference Fourier methods and a model for glycogen. J. molec. Biol. 156, 411423.
Goldsmith, E. J., Sprang, S. R., Hamlin, R., Xuong, N. & Fletterick, R. J. (1989). Domain separation in the activation of glycogen phosphorylase a. (Submitted to Science.)
Gopalakrishnan, P. V. & Karush, F. (1974). Antibody affinity. VII. Multivalent interaction of anti-lactoside antibody. J. Immunol. 113, 769778.
Gouaux, E. J. & Lipscomb, W. N. (1988). Three-dimensional structure of carbamoylphosphate and succinate bound to aspartate carbamoyltransferase. Proc. natn. Acad. Sci. U.S.A. 85, 42054208.
Graves, D. J. & Wang, J. H. (1972). α-glucan phosphorylases - chemical and physical basis of catalysis and regulation. In The Enzymes, (ed. Boyer, P. D.) vol. 7, PP. 435482. New York: Academic Press.
Gunsalus, R. P., Gunsalus, M. A. & Gunsalus, G. L. (1986). Intracellular trp repressor levels in Escherichia coli. J. Bacteriol. 167, 272278.
Hajdu, J., Acharya, K. R., Stuart, D. I., McLaughlin, P. J., Barford, D., Oikonomakos, N. G., Klein, H. & Johnson, L. N. (1987). Catalysis in the crystal: synchrotron radiation studies with glycogen phosphorylase b. EMBO J. 6, 539545.
Heidmann, T., Beuchardt, J., Neumann, E. & Changeux, J. P. (1983). Rapid kinetics of agonist binding and permeability response analysed in parallel on acetylcholine receptor-rich membranes from Torpedo marmorata. Biochemistry 22. 54525459.
Heidner, E. J., Frey, T. G., Held, J., Weissman, L. J., Fenna, R. E., Lei, M., Harel, M., Kabsch, H., Sweet, R. M. & Eisenberg, D. (1978). New crystal forms of glutamine synthetase and implications for the molecular structure. J. molec. Biol. 122, 163173.
Hellinga, H. W. & Evans, P. R. (1987). Mutations in the active site of Escherichia coli phosphofructokinase. Nature 327. 437439.
Helmreich, E. J. M. & Klein, H. W. (1980). The role of pyridoxal phosphate in the catalysis of glycogen phosphorylase. Angew. Chem. Int. Ed. Eng. 19, 441455.
Hendrickson, W. A. & Love, W. E. (1971). Structure of lamprey haemoglobin. Nature New Biol. 232, 197203.
Hervè, J. (1989). Aspartate transcarbamylase from E. coli. In Allosteric Enzymes (ed. Hervé, G.) CRC Press (in the Press).
Hervé, G., Moody, M. F., Tave, P., Vachette, P. & Jones, P. T. (1985). Quaternary structure changes in aspartate transcarbamylase by X-ray scattering. J. molec. Biol. 185, 189199.
Honzatko, R. B., Crawford, J. L., Monaco, H. L., Ladner, J. E., Edwards, B. F. P., Evans, D. R., Warren, S. G., Wiley, D. C., Ladner, R. C. & Lipscomb, W. N. (1982). Crystal and molecular structure of native and CTP-liganded aspartate carbamoyltransferase from Escherichia coli. J. molec. Biol. 160, 219263.
Honzatko, R. B. & Lipscomb, W. N. (1982). Interactions of phosphate ligands with Escherichia coli aspartate carbamoyltransferase in the crystalline state. j. molec. Biol. 160, 265286.
Howlett, G. J., Blackburn, M. N., Compton, J. G. & Schachman, H. K. (1977). Allosteric regulation of aspartate transcarbamylase. Analysis of the structural and functional behaviour in terms of a two-state model. Biochemistry 16. 50915099.
Howlett, G. J. & Schachman, H. K. (1977). Allosteric regulation of aspartate transcarbamylase. Changes in the sedimentation coefficient promoted by the bisubstrate analogue N-(phosphonacetyl)-L-aspartate. Biochemistry 16. 50775083.
Imai, K., (1982). Allosteric Effects in Haemoglobin. Cambridge University Press.
Jarvest, R. L., Lowe, G. & Potter, B. V. L. (1981). The stereochemical course of phosphoryl transfer catalyzed by Bacillus stearothermophilus and rabbit-muscle phosphofructokinase with a chiral [16O, 17O, 18O,]phosphate ester. Biochem.J. 199, 427432.
Joachimiak, A. J., Kelley, R. L., Gunsalus, R. P., Yanofsky, C. & Sigler, P. B. (1983). Purification and characterization of the trp aporepressor. Proc. natn. Acad. Sci. U.S.A. 80, 668672.
Johnson, B. A., Bonaventura, C. & Bonaventura, J. (1984). Allosteric modulation of Callinectes sapidus haemocyanin by lactate. Biochemistry 23. 872878.
Johnson, K. A., Olson, J. S. & Phillips, G. N. Jr. (1989). The structure of myoglobinethyl isocyanide: histidine as a swinging door for ligand entry. J. molec. Biol. 207, 459463.
Johnson, L. N., Hajdu, J., Acharya, K. R., Stuart, D. I., McLaughlin, P. J., Oikonomakos, N. G. & Barford, D. (1989). Glycogen phosphorylase b. In Allosteric Proteins (ed. Hervé, G.), CRC Press.
Jullien, L. & Lehn, J.-M. (1988). The “Chundle” approach to molecular channels: synthesis of a macrocycle-based molecular bundle. Tetrahedron Lett. 29 (31), 38033806.
Kantrowitz, E. R. & Lipscomb, W. N. (1988). Escherichia coli aspartate transcarbamylase: the relations between structure and function. Science 241. 669674.
Karush, F. (1978). The affinity of antibody: range, variability, and the role of multivalence. In Immunoglubulins (ed. Littman, G. W. and Good, R. A.), pp. 85115. Plenum.
Ke, H.-M., Honzatko, R. B. & Lipscomb, W. N., (1984). Structure of unligated aspartate carbamoyltransferase of Escherichia coli at 2·6 Å resolution. Proc. natn. Acad. Sci. U.S.A. 81, 40374040.
Ke, H., Lipscomb, W. N., Cho, Y. & Honzatko, R. B. (1988). Complex of N-phosphonyl-L-aspartate with aspartate carbamoyltransferase. X-ray refinement, analysis of conformational changes and catalytic and allosteric mechanisms. J. molec. Biol. 204, 725747.
Kelly, R. & Yanofsky, C. (1985). Mutational studies with the trp repressor of E. coli support the helix-turn-helix model of repressor recognition of operator DNA. Proc. natn. Acad. Sci. U.S.A. 82, 483487.
Kilmartin, J. V. (1974). Influence of DPG on the Bohr effect of human haemoglobin. FEBS Lett. 38, 147148.
Kilmartin, J. V., Breen, J. J., Roberts, G. C. K. & Ho, C. (1973). Direct measurement of the pK values of an alkaline Bohr group in human haemoglobin. Proc. natn. Acad. Sci. U.S.A. 70, 12461249.
Kim, K., Fettinger, J., Sessler, J. L., Cyr, M., Hugdahl, J., Collman, J. P. & Ibers, J. A. (1989). Structural characterisation of a sterically encumbered iron(II) porphyrin CO complex. J. Am. Chem. Soc. 111, 403405.
Klug, A. & Rhodes, D. (1987). ‘Zinc fingers’: a novel protein motif for nucleic acid recognition. Trends biochem. Sci. 12, 464469.
Knowles, J. (1980). Enzyme-catalyzed phosphoryl transfer reactions. An. Rev. Biochem. 49. 877918.
Koshland, D. E. (1959). In The Enzymes, 2nd ed. vol. 1 (ed. Boyer, P. D.Lardy, H. & Myrbäck, K.), pp. 305346. New York: Academic Press.
Koshland, D. E., Nemethy, G. & Filmer, D. (1966). Comparison of experimental binding data and theoretical models in proteins containing subunits. Biochemistry 5. 365385.
Kotlarz, D. & Buc, H. (1982). Phosphofructokinases from Escherichia coli. Methods Enzymol. 90, 6070.
Krause, K. L., Volz, K. W. & Lipscomb, W. N. (1987). 2·5 Å structure of aspartate carbamoyltransferase complexed with the bisubstrate analog N-(phosphonacetyl)-Laspartate. J. molec. Biol. 193, 527553.
Krebs, E. G. (1986). The enzymology of control by phosphoryìation. In The Enzymes, 3rd ed. vol. 17 (ed. Boyer, P. D. and Krebs, E. G.), pp. 320. New York: Academic Press.
Krüse, J., Krüse, K. M., Witz, J., Chauvin, C, Jacrot, B. & Tardieu, A. (1982). Divalent ion-dependent reversible swelling of tomato bushy stunt virus and organisation of the expanded virion. J. molec. Biol. 162, 393417.
Kuiper, H., Antonini, E. & Brunori, M. (1977). Kinetic control of cooperativity in the oxygen binding of Panulirus interruptus haemocyanin. J. molec. Biol. 116, 569576.
Kuiper, H., Forlani, L., Chiancone, E., Antonini, E., Brunori, M. & Wyman, J. (1979). Multiple linkage in Panulirus interruptus. Biochemistry 18. 58495854.
Kuiper, H., Gaastra, W., Beintema, J. J., van Bruggen, E. F. J., Schepman, A. M. H. & Drenth, J. (1975). Subunit composition, X-ray diffraction, amino acid analysis and oxygen binding behaviour of Panulirus interruptus hemocyanin. J. molec. Biol. 99, 619629.
Kuriyan, J., Wilz, S., Karplus, M. & Petsko, G. A. (1986). X-ray structure and refinement of carbonmonoxy (Fell)-myoglobin at 1·5 Å resolution. J. molec. Biol. 192, 133154.
Ladjimi, M. M. & Kantrowitz, E. R. (1988). A possible model for the concerted transition in Escherichia coli aspartate transcarbamylase as deduced from site-directed mutagenesis studies. Biochemistry 27. 276283.
Ladjimi, M. M., Middleton, S. A., Kellerher, K. S. & Kantrowitz, E. R. (1988). Relationship between domain closure and binding, catalysis and regulation in Escherichia coli aspartate transcarbamylase. Biochemistry 27. 268276.
Lakowicz, J. R. & Weber, G. (1973). Quenching of protein fluorescence by oxygen. Detection of structural fluctuations in proteins on the nanosecond time scale. Biochemistry 12. 41714179.
Lalezari, I., Rahbar, S., Lalezari, P., Fermi, G. & Perutz, M. F. (1988). LR16, a compound with potent effects on the oxygen affinity of hemoglobin, on blood cholesterol, and on low density lipoprotein. Proc. natn. Acad. Sci. U.S.A. 85, 61176121.
Lamy, J., Leclerc, M., Sizaret, P.-Y., Lamy, J., Miller, K. I., McParland, R. & van Holde, K. E. (1987). Octopus dofleini hemocyanin: structure of the seven-domain polypeptide chain. Biochemistry 26. 35093518.
Lau, F. T.-K. & Fersht, A. R. (1987). Conversion of allosteric inhibition to activation in phosphofructokinase by protein engineering. Nature 326. 811812.
Lau, F. T.-K., Fersht, A. R., Hellinga, H. W. & Evans, P. R. (1987). Site-directed mutagenesis in the effector site of Escherichia coli phosphofructokinase. Biochemistry 26. 41434148.
Lawson, C. & Sigler, P. B. (1988). The structure of trp pseudorepressor at 1·65 Å shows why indol propionate acts as a trp ‘inducer’. Nature 333. 869871.
Lawson, C. L., Zhang, R.-G., Schevitz, R. W., Otwinowski, Z., Joachimiak, A. & Sigler, P. B. (1988). Flexibility of the DNA-binding domains of trp repressor. Proteins 3. 1831.
Lear, J. D., Wasserman, Z. R. & DeGrade, W. F. (1988). Synthetic amphiphilic peptide models for protein ion channels. Science 240. 11771181.
Leonard, R. J., Labarca, C. G., Charnet, P., Davidson, N. & Lester, H. A. (1988). Evidence that the M2 spanning region lines the ion channel pore of the nicotinic receptor. Science 242. 15781581.
Liddington, R., Derewenda, Z., Dodson, G. & Harris, D. (1988). Structure of liganded T-state of haemoglobin identifies the origin of cooperative oxygen binding. Nature 331. 725728.
Linzen, B., Soeter, N. M., Riggs, A. F., Schneider, H.-J., Schartau, W., Moore, M. D., Yokota, E., Behrens, P. Q., Nakashima, H., Takagi, T., Nemoto, T., Vereijken, J. M., Bak, H. J., Beintema, J. J., Volbeda, A., Gaykema, W. P. J. & Hol, W. G. J. (1985). The structure of arthropod haemocyanins. Science N. Y. 229, 519524.
Louie, G., Tran, T., Englander, J. J. & Englander, S. W. (1988). Allosteric energy at the hemoglobin β-chain C-terminus studied by hydrogen exchange. J. molec. Biol. 201, 755764.
McGeoch, D., McGeoch, J. & Morse, D. (1973). Synthesis of tryptophan operon RNA in a cell-free system. Nature New Biol. 245, 137140.
McLaughlin, P. J., Stuart, D. I., Klein, H. W., Oinomakos, J. G. & Johnson, L. N. (1984). Substrate cofactor interactions for glycogen phosphorylase b: a binding study in the crystal with heptenitol and heptulose-2-phosphate. Biochemistry 23. 58625873.
Madsen, N. B. (1986). Glycogen phosphorylase. In The Enzymes, 3rd ed., vol. 17 (ed. Boyer, P. D. and Krebs, E. G.), pp. 366394. New York: Academic Press.
Manwell, C. (1960). Oxygen equilibrium of the brachiopod Lingula hemerythrin. Science 132, 550551.
Marmorstein, R. Q. & Sigler, P. B. (1988). Structure and mechanism of the trp repressor/operator system. In Nucleic Acids and Molecular Biology (ed. Eckstein, F.). Heidelberg. Springer-Verlag.
Marmorstein, R. Q., Joachimiak, A., Sprinzl, M. & Sigler, P. B. (1987). The structural basis for the interaction between L-tryptophan and the Escherichia coli trp aporepressor. J. biol. Chem. 262, 49224927.
Matsukawa, S., Itatani, Y., Mawatari, K., Shimokawa, Y. & Yoneyama, Y. (1978). Quantitative evaluation for the role β-146 His and β-143 His residues in the Bohr effect of human haemoglobin in the presence of 0·1 M chloride ion. J. biol. Chem. 259, 1147911486.
Messana, C, Cerdonio, M., Shenkin, P., Noble, R. W., Fermi, G., Perutz, R. N. & Perutz, M. F. (1978). Influence of quaternary structure of the globin on thermal spin equilibria in different methaemoglobin derivatives. Biochemistry 17. 36523662.
Middleton, S. A. & Kantrowitz, E. R. (1988). Function of arginine-234 and aspartic acid-271 in domain closure, cooperativity, and catalysis in Escherichia coli aspartate transcarbamylase. Biochemistry 27, 86538660.
Miller, K. I. (1985). Oxygen equilibria of Octopus dofleini hemocyanin. Biochemistry 24. 45824586.
Momenteau, M., Scheidt, W. R., Elgenbrot, C. W. & Reed, C. A. (1988). A deoxymyoglobin model with a sterically unhindered axial imidazole. J. Am. Chem. Soc. 110, 12071215.
Monod, J., Changeux, J. P. & Jacob, F. (1963). Allosteric proteins and molecular control systems. J. molec. Biol. 6, 306329.
Monod, J. & Cohen-Bazire, G. (1953). L'effet d'inhibition spécifique dans la biosynthése de la tryptophane-desmase chez Aerobacter aerogenus. C.r. hebd. séanc. Acad. Sci., Paris 236. 530532.
Monod, J. & Jacob, F. (1961). Genetic regulation mechanisms in the synthesis of proteins. J. molec. Biol. 3, 318356.
Monod, J., Wyman, J. & Changeux, J. P. (1965). On the nature of allosteric transitions: a plausible model. J. molec. Biol. 12, 88118.
Namba, K., Pattanayek, R. & Stubbs, G. (1989). Visualization of protein-nucleic acid interactions in a virus: refined structure of intact tobacco mosaic virus at 2·9 Å resolution by X-ray diffraction. J. molec. Biol. 208, 307325.
Newell, J. O., Markby, D. W. & Schachman, H. K. (1989). Cooperative binding of the bisubstrate analog N-(phosphonacetyl)-L-aspartate to aspartate transcarbamylase and the heterotropic effects of ATP and CTP. J. biol. Chem. 264, 24762481.
Oiki, S., Danho, W., Madison, V. & Montal, M. (1988). M2 δ, a candidate for the structure lining the ionic channel of the nicotinic cholinergic receptor. Proc. natn. Acad. Sci. U.S.A. 85, 87038707.
Olson, J. S., Mathews, A. J., Rohlfs, R. J., Springer, B. A., Edelberg, K. D., Sliger, S. G., Tame, J., Renaud, J.-P, & Nagai, K. (1988). The role of the distal histidine in myoglobin and haemoglobin. Nature 336. 265266.
Onan, K., Rebek, J., Costello, T. & Marshall, L. (1983). Allosteric effects: structural and thermodynamic origins and binding cooperativity in a subunit model. J. Am. Chem. Soc. 105, 67596760.
Otwinowski, Z., Schevitz, R. W., Zhang, R.-g., Lawson, C. L., Joachimiak, A., Marmorstein, R. Q., Luisi, B. & Sigler, P. B. (1988). The crystal structure of the trp repressor/operator complex at atomic resolution. Nature 335. 321329.
Palm, D., Klein, H. W., Schinzel, R., Buehner, M. & Helmreich, E. J. M. (1989). The role of pyroxidal 5′-Phosphate in glycogen phosphorylase catalysis. Submitted to Perspectives in Biochem.
Perrella, M., Sabionedda, L., Samaja, M. & Rossi-Bernardi, L. (1986). The intermediate compounds between human hemoglobin and carbon monoxide at equilibrium and during approach to equilibrium. J. biol. Chem. 261, 83918396.
Perrella, M., Colosimo, A., Benazzi, L., Samaja, M. & Rossi-Bernardi, L. (1988). Intermediate compounds between hemoglobin and carbonmonoxide under equilibrium conditions.Symposion on Oxygen Binding and Heme Proteins, Asilomar Conference Grounds, Pacific Grove,California.
Perutz, M. F. & Mathews, F. S. (1966). An X-ray study of azide methaemoglobin. J. molec. Biol. 21, 199202.
Perutz, M. F. (1970). Stereochemistry of cooperative effects in haemoglobin. Nature 228. 726739.
Perutz, M. F. (1979). Regulation of oxygen affinity of hemoglobin: influence of structure of the globirt on the heme. A. Rev. Biochem. 48, 327386.
Perutz, M. F. (1987). Molecular anatomy, physiology and pathology of hemoglobin. In The Molecular Basis of Blood Diseases (ed. Stamatoyannopoulos, G., Nienhuis, A. W., Leder, P. and Majerus, P. W.), pp. 127178. Philadelphia: W. B. Saunders.
Perutuz, M. F. (1988). Allosteric enzymes: control by phosphorylation. Nature 336. 202203.
Perutz, M. F., Fermi, G., Abraham, D. J., Poyart, C. & Bursaux, E. (1986). Hemoglobin as a receptor of drugs and peptides: X-ray studies of the stereochemistry of binding. J. Am. Chem. Soc. 108, 10641078.
Perutz, M. F., Fermi, G., Luisi, B., Shaanan, B. & Liddington, R. C. (1987). Stereochemistry of cooperative effects in hemoglobin. Accs. Chem. Res. 20, 309321.
Perutz, M. F., Kilmartin, J. V., Nishikura, K., Fogg, J. H., Butler, P. J. G. & Rollema, H. S. (1980). Identification of residues contributing to the Bohr effect of human haemoglobin. J. molec. Biol 138. 649670.
Perutz, M. F., Sanders, J. K. M., Chenery, D. H., Noble, R. W., Pennelly, R. R., Fung, L. W.-M., Ho, C, Giannini, I., Pörschke, D. & Winckler, H. (1978). Interactions between the quaternary structure of the globin and the spin state of the heme in ferric mixed spin derivatives of hemoglobin. Biochemistry 17. 36403652.
Phillips, S. E. V. & Schoenborn, B. P. (1981). Neutron diffraction reveals oxygenhistidine hydrogen bond in myoglobin. Nature 292. 8182.
Phillips, S. E. V., Mansfield, I., Parsons, I., Davidson, B. E., Rafferty, J. B., Somers, W. S., Margarita, D., Cohen, G. N., St.-Girons, I. & Stockley, P. G. (1989). Tandem overlapping binding of the E. coli methionine repressor. Nature (in the Press).
Philo, S. & Dreyer, U. (1985). Quarternary structure has little influence on spin states in mixed-spin human methemoglobins. Biochemistry 24. 29852991.
Ptashne, M. (1986). A Genetic Switch. Cambridge Mass.: Cell Press; Oxford: Blackwell Scientific Publications.
Rafferty, J. B., Somers, W. S., St.-Girons, I. & Phillips, S. E. V. (1989). Threedimensional crystal structures of E. coli met repressor with and without co-repressors. Nature (in the Press).
Rebek, J., Wattley, R. V., Costello, T., Gadwood, R. & Marshall, L. (1981). Allosterische Effekte: Bindungskooperativität in einer Modellverbindung mit Untereinheiten. Angew. Chemie 93. 584585.
Reem, R. C. & Solomon, E. I. (1987). Spectroscopic studies of the binuclear ferrous active site of deoxyhemerythrin; coordination number and probable bridging ligands for the native and ligand-bound forms. J. Am. Chem. Soc. 109, 12161226.
Remington, S., Wiegand, G. & Huber, R. (1982). Crystallographic refinement and atomic models of two different forms of citrate synthase at 2·7 Å and 1·7 Å resolution. J. molec. Biol. 158, 111152.
Richardson, D. E., Reem, R. C. & Solomon, E. I. (1983). Cooperativity in oxygen binding to Lingula reevii hemerythrin: spectroscopic comparisons to the sipunculid hemerythrin binuclear active site. J. Am. Chem. Soc. 105, 77807781.
Ringe, D., Petsko, G. E., Kerr, D. E. & De Montellano, F. R. O. (1984). Reaction of myoglobin with phenylhydrazine – a molecular doorstop. Biochemistry 23. 24.
Robert, C. H., Decker, H., Richey, B., Gill, S. J. & Wyman, J. (1987). Nesting: hierarchies of allosteric interactions. Proc. natn. Acad. Set. U.S.A. 84, 18911895.
Robinson, I. K. & Harrison, S. C. (1982). Structure of the expanded state of tobacco bushy stunt virus. Nature 297. 563568.
Rose, J. K., Squires, C. L., Yanofsky, C, Yang, H.-L. & Zubay, G. (1973). Regulation of in vitro transcription of the tryptophan operon by purified RNA polymerase in the presence of partially purified repressor and tryptophan. Nature New Biol. 245, 133137.
Schachman, H. K. (1988). Can a simple model account for the allosteric transition of aspartate transcarbamylase? J. biol. Chem. 263, 1858318586.
Scheidt, R. W. & Reed, C. A. (1981). Spin-state/stereochemical relationships in iron porphyrins: implications for the heme proteins. Chem. Rev. 81, 543555.
Schevitz, R. W., Otwinowski, Z., Joachimiak, A., Lawson, C. L. & Sigler, P. B. (1985). The three-dimensional structure of trp repressor. Nature 317. 782786.
Schirmer, T. & Evans, P. R. (1989). The crystal structure of the T-state of phosphofructokinase. (In preparation.)
Schleif, R. (1988). DNA binding to proteins. Science 241. 11821187.
Shaanan, B. (1983). Structure of human oxyhaemoglobin at 2·1 Å resolution. J. molec. Biol. 171, 3150.
Shepherdson, M. & Pardee, A. B. (1960). Production and crystallization of aspartate transcarbamylase. J. biol. Chem. 235, 32333237.
Sheriff, S., Hendrickson, W. A. & Smith, J. L. (1987). Structure of myohemerythrin in the azidomet state at 1·7/1·3 Å resolution. J. molec. Biol. 197, 273296.
Shiemke, A. K., Loehr, T. M. & Sanders-Loehr, J. (1984). Resonance Raman study of the μ-oxo bridged binuclear iron center in oxyhemerythrin. J. Am. Chem. Soc. 106, 49514956.
Shirakihara, Y. & Evans, P. R. (1988). Crystal structure of the complex of phosphofructokinase from Escherichia coli with its reaction products. J. molec. Biol. 204, 973994.
Sprang, S. R., Acharya, K. R., Goldsmith, E. J., Stuart, D. I., Varvill, K., Fletterick, R. J., Madsen, N. B. & Johnson, L. N. (1988). Structural changes in glycogen phosphorylase induced by phosphorylation. Nature 336. 215221.
Springer, B. A., Egeberg, K. D., Sugar, S. G., Rohlfs, R. J., Mathews, A. J. & Olson, J. S. (1989). Discrimination between oxygen and carbon monoxide and inhibition of autoxidation by myoglobin: site-directed mutagenesis of the distal histidine. J. biol. Chem. 264, 30573060.
Springer, B. A., Egeberg, K. D., Sugar, S. G., Rohlfs, R. J., Mathews, A. J. & Olson, J. S. (1989). Site-directed mutagenesis of sperm whale myoglobin: role of His E7 and Val E11 in ligand binding. J. biol. Chem. (In the press.)
Stadtman, E. R. & Ginsburg, A. (1974). The glutamine synthetase of Escherichia colt: structure and control. In The Enzymes, vol. 10, pp. 755808. New York: Academic Press.
Stencamp, R. E., Sieker, L. C., Jensen, L. H., McCallum, J. D. & Sanders-Loehr, J. (1985). Active site structures of deoxyhemerythrin and oxyhemerythrin. Proc. natn. Acad. Sci. U.S.A. 82, 713716.
Szabo, A. (1978). The kinetics of haemoglobin and transition state theory. Proc. natn. Acad. Sci. U.S.A. 75, 21082111.
Tauc, P., Vachette, P., Middleton, S. A. & Kantrowitz, E. R. (1989). Structural consequences of the replacement of Glu-239 by Gin in the catalytic chain of Escherichia coli aspartate transcarbamylase. Submitted to J. molec. Biol.
Toyoshima, C. & Unwin, N. (1988). Ion channel of acetylcholine receptor reconstructed from images of postsynaptic membranes. Nature 336. 247250.
Trautmann, A. (1984). A comparative study of the activation of the cholinergic receptor by various agonists. Proc. R. Soc. Lond. 218, 241251.
Umbarger, E. & Brown, B. (1958). Isoleucine and valine metabolism in Escherichia coli. VII. The negative feedback mechanism controlling isoleucine synthesis. J. biol. Chem. 233. 415420.
Unwin, P. N. T. (1987). Design and action of cell communication channels. Chemica Scripta 27B, 4751.
Unwin, P. N. T. & Ennis, P. D. (1984). Two configurations of a channel-forming membrane protein. Nature 307. 609613.
Unwin, P. N. T., Toyoshima, C. & Kubalek, E. (1988). Arrangement of the acetylcholine receptor subunits in the resting and desensitized states, determined by cryoelectron microscopy of crystallized Torpedo postsynaptic membranes. J. Cell Biol. 107, 11231138.
Unwin, P. N. T. & Zampighi, G. (1980). Structure of the junction between communicating cells. Nature 283, 545.
Van Holde, K. E. & Miller, K. I. (1982). Haemocyanins. Q. Rev. Biophys. 15, 1129.
Volbeda, A. & Hol, W. (1989 a). Pseudo-twofold symmetry in the copper-binding domain of arthropodan hemocyanins: possible implications for the evolution of oxygen transport proteins. J. molec. Biol. 206, 531546.
Volbeda, A. & Hol, W. (1989 b). Crystal structure of hemocyanin from Panulirus interruptus refined at 3·2 Å resolution. J. molec. Biol. 208, in the press.
Watson, H. C. & Kendrew, J. C. (1961). Comparison between the amino-acid sequences of sperm whale myoglobin and of human haemoglobin. Nature 190. 670672.
Weber, K. (1968). A new structural model of Escherichia coli aspartate transcarbamylase and the amino acid sequence of the regulatory chain. Nature 218. 11161119.
Wente, S. R. & Schachman, H. K. (1987). Shared active sites in oligomeric enzymes: model studies with defective mutants of aspartate transcarbamylase produced by sitedirected mutagenesis. Proc. natn. Acad. Sci. U.S.A. 84, 3135.
Werner, W. E., Cann, J. R. & Schachman, H. K. (1989). Boundary spreading in sedimentation velocity experiments on partially liganded aspartate transcarbamylase. A ligand-mediated isomerization. J. molec. Biol. 206, 231238.
Werner, W. E. & Schachman, H. K. (1989). Analysis of the ligand-promoted conformational change in aspartate transcarbamylase: evidence for a two-state transition from boundary spreading in sedimentation velocity experiments. J. molec. Biol. 206, 221230.
Wiley, D. C. & Lipscomb, W. (1968). Crystallographic determination of the symmetry of aspartate transcarbamylase. Nature 218. 11191121.
Wyman, J. (1967). Allosteric linkage. J. Am. Chem. Soc. 89, 22022218.
Wyman, J. (1984). Linkage graphs: a study in the thermodynamics of macromolecules. Q. Rev. Biophys. 17, 453488.
Yamashita, M. M., Almassy, R. J., Janson, C. A., Cascio, D. & Eisenberg, D. (1989). Refined atomic model of glutamine synthetase at 3·5 Å resolution. J. biol. Chem. (In the Press.)
Yates, R. A. & Pardee, A. B. (1956). Control of pyrimidine biosynthesis in Escherichia coli by a feedback mechanism. J. biol. Chem. 221, 757770.
Zhang, K., Stern, E. A., Ellis, F., Sanders-Loehr, J. & Shiemke, A. K. (1988). The active site of hemerythrin as determined by X-ray Absorption Fine Structure. Biochemistry 27. 74707479.
Zhang, R.-g, Joachimiak, A., Lawson, C. L., Schevitz, R. W., Otwinowski, Z. & Sigler, P. B. (1987). The crystal structure of trp aporepressor at 1·8 Å shows how binding tryptophan enhances DNA affinity. Nature 327. 591597.
Zubay, G., Morse, D. E., Schrenk, W. J. & Miller, J. H. M. (1972). Detection and isolation of the repressor protein for the tryptophan operator of Escherichia coli. Proc. natn. Acad. Sci. U.S.A. 69, 11001103.


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