| Literature DB >> 22684058 |
Jing Hou1, Kamila Wojciechowska, Heping Zheng, Maksymilian Chruszcz, David R Cooper, Marcin Cymborowski, Tatiana Skarina, Elena Gordon, Haibin Luo, Alexei Savchenko, Wladek Minor.
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.Entities:
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Year: 2012 PMID: 22684058 PMCID: PMC3370898 DOI: 10.1107/S1744309112017939
Source DB: PubMed Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun ISSN: 1744-3091