Structure of a short-chain dehydrogenase/reductase from Bacillus anthracis.
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.
Molecular Physiology and Biological Physics, University of Virginia, 1340 Jefferson Park Avenue, Jordan Hall, Room 4223, Charlottesville, VA 22908, USA.
Jing
J
Hou
Kamila
K
Wojciechowska
Heping
H
Zheng
Maksymilian
M
Chruszcz
David R
DR
Cooper
Marcin
M
Cymborowski
Tatiana
T
Skarina
Elena
E
Gordon
Haibin
H
Luo
Alexei
A
Savchenko
Wladek
W
Minor
D001408:Bacillus anthracis / Q000201:enzymology*; D001665:Binding Sites; D055162:Biocatalysis; D008958:Models, Molecular; D010088:Oxidoreductases / Q000737:chemistry*; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D040681:Structural Homology, Protein; D013379:Substrate Specificity
D010088:Oxidoreductases