Hostname: page-component-848d4c4894-5nwft Total loading time: 0 Render date: 2024-06-01T19:09:45.985Z Has data issue: false hasContentIssue false
  • English
  • Français

Pig heart short chain l-3-hydroxyacyl-CoA dehydrogenase revisited: Sequence analysis and crystal structure determination

Published online by Cambridge University Press:  01 October 1999

JOSEPH J. BARYCKI ,
LAURIE K. O'BRIEN ,
JENS J. BIRKTOFT ,
ARNOLD W. STRAUSS  and
LEONARD J. BANASZAK
JOSEPH J. BARYCKI
Affiliation:
Department of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Minneapolis, Minnesota 55455
LAURIE K. O'BRIEN
Affiliation:
Department of Pediatrics, Washington University, School of Medicine, St. Louis, Missouri 63110
JENS J. BIRKTOFT
Affiliation:
X-taldesigns, Box 20620, New York, New York 10025
ARNOLD W. STRAUSS
Affiliation:
Department of Pediatrics, Washington University, School of Medicine, St. Louis, Missouri 63110
LEONARD J. BANASZAK
Affiliation:
Department of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Minneapolis, Minnesota 55455
Get access

Abstract

Short chain l-3-hydroxyacyl CoA dehydrogenase (SCHAD) is a soluble dimeric enzyme critical for oxidative metabolism of fatty acids. Its primary sequence has been reported to be conserved across numerous tissues and species with the notable exception of the pig heart homologue. Preliminary efforts to solve the crystal structure of the dimeric pig heart SCHAD suggested the unprecedented occurrence of three enzyme subunits within the asymmetric unit, a phenomenon that was thought to have hampered refinement of the initial chain tracing. The recently solved crystal coordinates of human heart SCHAD facilitated a molecular replacement solution to the pig heart SCHAD data. Refinement of the model, in conjunction with the nucleotide sequence for pig heart SCHAD determined in this paper, has demonstrated that the previously published pig heart SCHAD sequence was incorrect. Presented here are the corrected amino acid sequence and the high resolution crystal structure determined for pig heart SCHAD complexed with its NAD+ cofactor (2.8 Å; Rcryst = 22.4%, Rfree = 28.8%). In addition, the peculiar phenomenon of a dimeric enzyme crystallizing with three subunits contained in the asymmetric unit is described.

Keywords

β-oxidationdehydrogenaseprimary sequenceSCHADX-ray structure
Type
Research Article
Information
Protein Science , Volume 8 , Issue 10 , October 1999 , pp. 2010 - 2018
Copyright
© 1999 The Protein Society

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)