3icc
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Crystal structure of a putative 3-oxoacyl-(acyl carrier protein) reductase from Bacillus anthracis at 1.87 A resolution
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Structural highlights
FunctionEvolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe crystal structure of a short-chain dehydrogenase/reductase from Bacillus anthracis strain `Ames Ancestor' complexed with NADP has been determined and refined to 1.87 A resolution. The structure of the enzyme consists of a Rossmann fold composed of seven parallel beta-strands sandwiched by three alpha-helices on each side. An NADP molecule from an endogenous source is bound in the conserved binding pocket in the syn conformation. The loop region responsible for binding another substrate forms two perpendicular short helices connected by a sharp turn. Structure of a short-chain dehydrogenase/reductase from Bacillus anthracis.,Hou J, Wojciechowska K, Zheng H, Chruszcz M, Cooper DR, Cymborowski M, Skarina T, Gordon E, Luo H, Savchenko A, Minor W Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Jun 1;68(Pt 6):632-7. Epub, 2012 May 24. PMID:22684058[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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This page was last modified 06:19, 27 November 2024.