Structural highlights
Publication Abstract from PubMed
The uropathogenic Escherichia coli strain CFT073 contains multiple iron and heme transport systems, which facilitate infection of the host urinary tract. To elucidate the molecular and cellular function of ChuY, a hypothetical gene in the heme degradation/utilization pathway, we solved the crystal structure of ChuY at 2.4 A resolution. ChuY has high structural homology with human biliverdin and flavin reductase. We confirmed that ChuY has flavin mononucleotide (FMN) reductase activity, using NAD(P)H as a cofactor, and shows porphyrin ring binding affinity. A chuY deletion-insertion strain showed reduced survival potential compared to wild-type and complemented strains in mammalian cells. Current results suggest ChuY acts as a reductase in heme homeostasis to maintain the virulence potential of E. coli CFT073.
Structural and functional study of ChuY from Escherichia coli strain CFT073.,Kim H, Chaurasia AK, Kim T, Choi J, Ha SC, Kim D, Kim KK Biochem Biophys Res Commun. 2017 Jan 22;482(4):1176-1182. doi:, 10.1016/j.bbrc.2016.12.008. Epub 2016 Dec 3. PMID:27919686[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kim H, Chaurasia AK, Kim T, Choi J, Ha SC, Kim D, Kim KK. Structural and functional study of ChuY from Escherichia coli strain CFT073. Biochem Biophys Res Commun. 2017 Jan 22;482(4):1176-1182. doi:, 10.1016/j.bbrc.2016.12.008. Epub 2016 Dec 3. PMID:27919686 doi:http://dx.doi.org/10.1016/j.bbrc.2016.12.008
