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International Union of Crystallography, Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 6(68), p. 632-637

DOI: 10.1107/s1744309112017939

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Structure of a short-chain dehydrogenase/reductase fromBacillus anthracis

Journal article published in 2012 by Jing Hou, Kamila Wojciechowska, Heping Zheng, Maksymilian Chruszcz ORCID, David R. Cooper, Marcin Cymborowski, Tatiana Skarina, Elena Gordon, Haibin Luo, Alexei Savchenko, Wladek Minor ORCID
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This paper is available in a repository.

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Abstract

The 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 Å resolution. The structure of the enzyme consists of a Rossmann fold composed of seven parallel β-strands sandwiched by three α-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.