Open AccessPreliminary X‐ray diffraction analysis of YqjH from Escherichia coli : a putative cytoplasmic ferri‐siderophore reductase
Author(s) -
Bamford Vicki A.,
Armour Maria,
Mitchell Sue A.,
Cartron Michaël,
Andrews Simon C.,
Watson Kimberly A.
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430910802352x
Subject(s) - shewanella putrefaciens , escherichia coli , siderophore , fumarate reductase , oxidoreductase , biology , biochemistry , homology modeling , chemistry , enzyme , bacteria , gene , genetics
YqjH is a cytoplasmic FAD‐containing protein from Escherichia coli ; based on homology to ViuB of Vibrio cholerae , it potentially acts as a ferri‐siderophore reductase. This work describes its overexpression, purification, crystallization and structure solution at 3.0 Å resolution. YqjH shares high sequence similarity with a number of known siderophore‐interacting proteins and its structure was solved by molecular replacement using the siderophore‐interacting protein from Shewanella putrefaciens as the search model. The YqjH structure resembles those of other members of the NAD(P)H:flavin oxidoreductase superfamily.