Preliminary X-ray diffraction analysis of YqjH from Escherichia coli: a putative cytoplasmic ferri-siderophore reductaseTools  Bamford, V. A., Armour, M., Mitchell, S. A., Cartron, M., Andrews, S. C. and Watson, K. A. (2008) Preliminary X-ray diffraction analysis of YqjH from Escherichia coli: a putative cytoplasmic ferri-siderophore reductase. Acta Crystallographica Section F-Structural Biology and Crystallization Communications, 64 (9). pp. 792-796. ISSN 1744-3091
To link to this article DOI: 10.1107/S174430910802352X Abstract/SummaryYqjH 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 A 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.
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