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Biophysics of the structure and function of porins

  • Bing K. Jap (a1) and Peter J. Walian (a1)
  • DOI:
  • Published online: 01 March 2009

Gram-negative bacteria such as Escherichia coli (E. coli) and Salmonella typhimurium (S. typhimurium) have two layers of membranes in the cellular envelope – the cytoplasmic membrane and the outer membrane (Fig. I). Between these membranes is a periplasmic space in which there is a peptidoglycan layer that provides the cells with mechanical rigidity. In this periplasmic space, there are also a variety of hydrolases and binding proteins. The composition of the outer membrane is somewhat unusual. This membrane bilayer is asymmetric, having an inner (periplasmic) leaflet composed of phospholipids and an outer (extracellular) leaflet formed by lipopolysaccharide (LPS). Unlike phospholipids having two acyl chains, LPS has six or seven saturated fatty acid chains (see reviews, Lugtenberg & Van Alphen, 1983; Nikaido & Vaara, 1985; Nakae, 1986). The head groups of LPS have a strong affinity for divalent cations such as Ca2+, and given a sufficient concentration of these ions the outer membrane can form quite a formidable permeability barrier through this head group/salt bridge network (Nikaido & Vaara, 1985). The function of the outer membrane is to serve as a protective envelope against hostile environments such as those in the intestinal tract of animals where harmful and toxic substances - for example, bile salts and various enzymes - are often found. The outer membrane itself would be impermeable to most hydrophilic solutes were it not for the presence of membrane channels. The presence of a large number of pore-forming proteins provides both specific and nonspecific diffusion pathways across the outer membrane for solutes such as nutrients and waste products to diffuse into or out of the cell.

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K. Bauer , A. Schmid , W. Boos , R. Benz & J. Tommassen (1988 a) Pore formation by pho-controlled outer-membrane proteins of various Enterobacteriaceae in lipid bilayers. Eur.J. Biochem. 174, 199205.

E. Beck & E. Bremer (1980) Nucleotide sequence of the gene omp A coding the outer membrane protein II* of Escherichia coli K-iz. Nucl. Acids Res. 8, 30113024.

S. A. Benson , J. L. L. Occi & B. A. Sampson (1988) Mutations that alter the pore function of the OmpF porin of Escherichia coli K12. J. molec. Biol. 203, 961970.

R. Benz (1985) Porin from bacterial and mitochondrial outer membranes. CRC crit. Rev. Biochem. 19, 2, 145190.

R. Benz (1988) Structure and function of porins from Gram-negative bacteria. Ann. Rev. Microbiol. 42, 359393.

C. Berrier , A. Coulombe , C. Houssin & A. Ghazi (1989) A patch-clamp study of ion channels of inner and outer membranes and of contact zones of E. coli, fused into giant liposomes. FEBS Lett. 259, 2732.

D. Bosch , J. Leunissen , J. Verbakel , M. De Jong , H. Van Erp & J. Tommassen (1986) Periplasmic accumulation of truncated forms of outer-membrane PhoE protein of Escherichia coli K-12. J. molec. Biol. 189, 449455.

D. Bosch & J. Tommassen (1987) Effects of linker insertions on the biogenesis and functioning of the Escherichia coli outer membrane pore protein PhoE. Molec. gen. Genet. 208, 485489.

V. Braun (1975) Covalent lipoprotein from the outer membrane of Escherichia coli. Biochim. biophys. Acta 415, 335377.

V. Braun , H. Rotering , J.-P. Ohms & H. Hagenmaier (1976) Conformational studies on murein lipoprotein from the outer membrane of Escherichia coli. Eur. J. Biochem. 70, 601610.

C.-F. Chang , S. Mizushima & R. M. Glaeser (1985) Projected structure of the pore-forming OmpC protein from Escherichia coli outer membrane. Biophys. J. 47, 629639.

R. Chen , C. Krämer , W. Schmidmayr , U. Chen-Schmeisser & U. Henning (1982) Primary structure of major outer-membrane protein I (OmpF protein, Porin) of Escherichia coli B/r. Biochem. J. 203, 3343.

R. Chen , W. Schmidmayr , C. Krämer , U. Chen-Schmeisser & U. Henning (1980) Primary structure of major outer membrane protein II* (OmpA protein) of Escherichia coli K-12. Proc. natn. Acad. Sci. USA 77, 45924596.

P. Y. Chou & G. D. Fasman (1978) Empirical predictions of protein conformation. Ann. Rev. Biochem. 47, 251276.

J. M. Clément & M. Hofnung (1981) Gene sequence of the λ receptor, an outer membrane protein of E. coli K12. Cell 27, 507514.

I. Chopra (1988) Molecular mechanisms involved in the transport of antibiotics into bacteria. Parasitology. 96, S25S44.

R. P. Darveau , R. E. W. Hancock & R. Benz (1984) Chemical modification of the anion selectivity of the PhoE porin from the Escherichia coli outer membrane. Biochim. biophys. Acta. 774, 6774.

N. G. Davis & P. Model (1985) An artificial anchor domain: hydrophobicity suffices to stop transfer. Cell. 41, 607614.

A. H. Delcour , B. Martinac , J. Adler & C. Kung (1989) Modified reconstitution method used in patch-clamp studies of Escherichia coli ion channels. Biophys. J. 56, 631636.

D. L. Dorset , A. Engel , M. Häner , A. Massalski & J. P. Rosenbusch (1983) Two-dimensional crystal packing of matrix porin. A channel forming protein in Escherichia coli outer membranes. J. molec. Biol. 165, 701710.

D. L. Dorset , A. Engel , A. Massalski & J. P. Rosenbusch (1984) Three dimensional structure of a membrane pore. Electron microscopical analysis of Escherichia coli outer membrane. Biophys. J. 45, 128129.

G. Ehrenstein , H. Lecar & R. Nossal (1970) The nature of the negative resistance in bimolecular lipid membranes containing excitability-inducing material. J. gen. Physiol. 55, 119133.

G. Eisenman & J. A. Dani (1987) An introduction to molecular architecture and permeability of ion channels. Ann. Rev. Biophys. biophys. Chem. 16, 205226.

A. Engel , A. Massalski , H. Schindler , D. L. Dorset & J. P. Rosenbusch (1985) Porin channel triplets merge into single outlets in Escherichia coli outer membranes. Nature. 317, 643645.

R. Freudl & S. T. Cole (1983) Cloning and molecular characterization of the omp A gene from Salmonella typhimurium. Eur. J. Biochem. 134, 497502.

R. M. Garavito , J. Jenkins , J. N. Jansonius , R. Karlsson & J. P. Rosenbusch (1983) X-ray diffraction analysis of matrix porin, an integral membrane protein from Escherichia coli outer membranes. J. molec. Biol. 164, 313327.

R. M. Garavito & J. P. Rosenbusch (1980) Three-dimensional crystals ofan integral membrane protein: an initial X-ray analysis. J. Cell Biol. 86, 327329.

M. N. Hall & T. J. Silhavy (1981) Genetic analysis of the ompB locus in Escherichia coli K-12. J. molec. Biol. 151, 115.

R. E. W. Hancock , A. Schmidt , K. Bauer & R. Benz (1986) Role of lysines in ion selectivity of bacterial outer membrane porins. Biochim. biophys. Acta. 860, 263267.

S. Ichihara & S. Mizushima (1979) Arrangement of proteins O-8 and O-9 in outer membrane of Escherichia coli K-12.Existence of and heterotrimers. Eur. J Biochem. 100, 321328.

K. Inokuchi , N. Mutoh , S. Matsuyama & S. Mizushima (1982) Primary structure of the ompF gene that codes for a major outer membrane protein of Escherichia coli K-12. Nucl. Acids Res. 10, 69576968.

B. K. Jap (1988) High-resolution electron diffraction of reconstituted PhoE porin. J. molec. Biol. 199, 229231.

B. K. Jap (1989) Molecular design of PhoE porin and its functional consequences. J. molec. Biol. 205, 407419.

J. Korteland , J. Tommassen & B. Lugtenberg (1982) PhoE protein pore of the outer membrane Escherichia coli K12 is a particularly efficient channel for organic and inorganic phosphate. Biochim. biophys. Acta. 690, 282289.

J. Korteland , P. De Graaff & B. Lugtenberg (1984) PhoE protein pores in the outer membrane of Escherichia coli K-12 not only have a preference for P1 and p1-containing solutes but are general anion-preferring channels. Biochim. biophys. Acta 778, 311316.

J. Korteland , N. Overbeeke , P. De Graaff , P. Overduin & B. Lugtenberg (1985) Role of the Arg158 residue of the outer membrane PhoE pore protein of Escherichia coli K12 in bacteriophage TC45 recognition and in channel characteristics. Eur. J. Biochem. 152, 691697.

J. H. Lakey & F. Pattus (1989) The volatge-dependent activity of Escherichia coli porins in different planar bilayer reconstitutions. Eur. J. Biochem. 186, 303308.

D. M. Livermore (1988) Permeation of β-lactam antibiotics into Escherichia coli, Pseudomonas aeruginosa, and other Gram-negative bacteria. Rev. infect. Dis. 10, 691698.

M. Luckey & H. Nikaido (1980) Specificity of diffusion channels produced by λ phage receptor protein of Escherichia coli. Proc. natn. Acad. Sci. USA 77, 167171.

B. Lugtenberg & L. Van Alphen (1983) Molecular architecture and functioning of the outer membrane of Escherichia coli and other Gram-negative bacteria. Biochim. biophys. Acta. 737, 51115.

B. Lugtenberg , R. Peters , H. Bernheimer & W. Berendsen (1976) Influence of cultural conditions and mutations on the composition of the outer membrane proteins of Escherichia coli. Molec gen. Genet. 147, 251262.

P. A. Manning , A. P. Pugsley & P. Reeves (1977) Defective growth functions in mutants of Escherichia coli K12 lacking a major outer membrane protein. J. molec. Biol. 116, 285300.

A. Mauro , M. Blake & P. Labarca (1988) Voltage gating of conductance in lipid bilayers induced by porin from outer membrane of Neisseria gonorrhoeae. Proc. natn. Acad. Sci. USA 85, 10711075.

T. Mizuno , H. Kasai & S. Mizushima (1987) Construction of a series ompC–ompF chimeric genes by in vivo homologous recombination in Escherichia coli and characterization of their translational products. Molec. gen. Genet. 207, 217223.

R. Morona , J. Tommassen & U. Henning (1985) Demonstration of a bacteriophage receptor site on the Escherichia coli K12 outer-membrane protein OmpC by the use of a protease. Eur. J. Biochem. 150, 161169.

E. Nabedryk , R. M. Garavito & J. Breton (1988) The orientation of β-sheets in porin. A polarized Fourier transform infrared spectroscopie investigation. Biophys. J. 53, 671676.

T. Nakae (1976 a). Identification of the outer membrane protein of E. coli that produces transmembrane channels in reconstituted vesicle membranes. Biochem. biophys. Res. Commun. 71, 877884.

T. Nakae (1986) Outer-membrane permeability of bacteria. CRC crit. Rev. Microbiol. 13, 162.

A. Nakamura , D. N. Osterovsky , T. Miyazawa & S. Mizushima (1974) Infrared spectra of outer and cytoplasmic membranes of Escherichia coli. Biochim. biophys. Acta 332, 329335.

U. Nestel , T. Wacker , D. Woitzik , J. Weckesser , W. Kreutz & W. Welte (1989) Crystallization and preliminary X-ray analysis of porin from Rhodobacter capsulatus. FEBS Lett. 242, 405408.

H. Nikaido (1983) Proteins forming large channels from bacterial and mitochondria! outer membranes: porins and phage lambda receptor protein. Methods Enzymol. 97, 85100.

H. Nikaido & E. Y. Rosenberg (1981) Effect of solute size on diffusion rates through the transmembrane pores of the outer membrane of Escherichia coli. J. gen. Physiol. 77, 121135.

H. Nikaido & H. C. P. Wu (1984) Amino acid sequence homology among the major outer membrane proteins of Escherichia coli. Proc. natn. Acad. Sci. USA 81, 10481052.

M. J. Osborn (1969) Structure and biosynthesis of the bacterial cell wall. Ann. Rev. Biochem. 38, 501538.

N. Overbeeke & B. Lugtenberg (1980) Expression of outer membrane protein e of Escherichia coli K12 by phosphate limitation. FEBS Lett. 112, 229232.

N. Overbeeke , H. Bergmans , F. Van Mansfeld & B. Lugtenberg (1983) Complete nucleotide sequence of phoE, the structural gene for the phosphate limitation inducible outer membrane pore protein of Escherichia coli K12. J. molec. Biol. 163, 513532.

M. G. P. Page & J. P. Rosenbusch (1986) Topographic labelling of pore-forming proteins from the outer membrane of Escherichia coli. Biochem. J. 235, 651661.

E. T. Palva (1979) Protein interactions in the outer membrane of Escherichia coli. Eur. J. Biochem. 93, 495503.

W. J. Rocque & E. J. McGroarty (1989) Isolation and preliminary characterization of wild-type OmpC porin dimers from Escherichia coli K-12. Biochemistry 28, 37383743.

H. J. Sass , G. Büldt , E. Beckmann , F. Zemlin , M. Van Heel , E. Zeitler , J. P. Rosenbusch , D. L. Dorset & A. Massalski (1989) Densely packed β-structure at the protein—lipid interface of porin is revealed by high-resolution cryo-electron microscopy. J. molec. Biol. 209, 171175.

S. J. Schein , M. Colombini & A. Finkelstein (1976) Reconstitution in planar lipid bilayers of a voltage-dependent anion-selective channel obtained from paramecium mitochondria. J. membrane Biol. 30, 99120.

H. Schindler & J. P. Rosenbusch (1978) Matrix protein from Escherichia coli outer membranes forms voltage-controlled channels in lipid bilayers. Proc. natn. Acad. Sci. USA 75, 37513755.

H. Schindler & J. P. Rosenbusch (1981) Matrix protein in planar membranes: clusters of channels in a native environment and their functional reassembly. Proc. natn. Acad. Sci. USA. 78, 23022306.

M. Schindler & J. P. Rosenbusch (1982) Chemical modification of matrix porin from Escherichia coli: probing the pore topology of a transmembrane protein. J. Cell Biol. 92, 742746.

M. Schindler & J. P. Rosenbusch (1984) Structural transitions of porin, a transmembrane protein. FEES Lett. 173, 8589.

A. C. Steven , B. Ten Heggeler , R. Müller , J. Kistler & J. P. Rosenbusch (1977) Ultrastructure of a periodic protein layer in the outer membrane of Escherichia coli. J. cell Biol. 72, 292301.

J. Tommassen , P. De Geus , B. Lugtenberg , J. Hackett & P. Reeves (1982) Regulation of the pho regulon of Escherichia coli K-12. Cloning of the regulatory genes phoB and phoR and identification of their gene products. J. molec. Biol. 157, 265274.

J. Tommassen , A. P. Pugsley , J. Korteland , J. Verbakel & B. Lugtenberg (1984) Gene encoding a hybrid OmpF-PhoE pore protein in the outer membrane of Escherichia coli K12. Molec. gen. Genet. 197, 503508.

V. Vachon , R. Laprade & J. W. Coulton (1986) Properties of the porin of Haemophilus influenzae type b in planar lipid bilayer membranes. Biochim. biophys. Acta. 861, 7482.

P. Van Der Ley , P. Burm , M. Agterberg , J. Van Meersbergen & J. Tommassen (1987 b) Analysis of structure-function relationships in Escherichia coli K12 outer membrane porins with the aid of ompC-phoE and phoE-ompC hybrid genes. Molec. gen. Genet. 209, 585591.

A. Venegas , I. Gómez , I. Zaror & A. Yudelevich (1988) The nucleotide sequence of the Salmonella typhi ompC porin gene. Nucl. Acids Res. 16, 7721.

H. Vogel & F. Jähnig (1986) Models for the structure of outer-membrane proteins of Escherichia coli derived from raman spectroscopy and prediction methods. J. molec. Biol. 190, 191199.

M. S. Weiss , T. Wacker , U. Nestel , D. Woitzik , J. Weckesser , W. Kreutz , W. Welte & G. E. Schulz (1989) The structure of porin from Rhodobactercapsulatus at 0·6 nm resolution. FEBS Lett. 256, 143146.

K. R. Wong & J. T. Buckley (1989) Proton motive force involved in protein transport across the outer membrane of Aeromonas salmonicida. Science 246, 654656.

G. Xu , B. Shi , E. J. McGroarty & H. T. Tien (1986) Channel-closing activity of porins from Escherichia coli in bilayer lipid membranes. Biochim. biophys. Acta. 862, 5764.

H. Yamada & S. Mizushima (1980) Interaction between major outer membrane protein (O-8) and lipopolysaccharide in Escherichia coli K12. Eur. J. Biochem. 103, 209218.

J. D.-E. Young , M. Blake , A. Mauro & Z. A. Cohn (1983) Properties of the major outer membrane protein from Neisseria gonorrhoeae incorporated into model lipid membranes. Proc. natn. Acad. Sci. USA 80, 38313835.

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