
Structure of a short‐chain dehydrogenase/reductase from Bacillus anthracis
Author(s) -
Hou Jing,
Wojciechowska Kamila,
Zheng Heping,
Chruszcz Maksymilian,
Cooper David R.,
Cymborowski Marcin,
Skarina Tatiana,
Gordon Elena,
Luo Haibin,
Savchenko Alexei,
Minor Wladek
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309112017939
Subject(s) - bacillus anthracis , reductase , microbiology and biotechnology , chemistry , biochemistry , enzyme , biology , bacteria , genetics
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.