Publication Abstract from PubMed
BACKGROUND: The yffB (PA3664) gene of Pseudomonas aeruginosa encodes an uncharacterized protein of 13 kDa molecular weight with a marginal sequence similarity to arsenate reductase from Escherichia coli. The crystal structure determination of YffB was undertaken as part of a structural genomics effort in order to assist with the functional assignment of the protein. RESULTS: The structure was determined at 1.0 A resolution by single-wavelength anomalous diffraction. The fold is very similar to that of arsenate reductase, which is an extension of the thioredoxin fold. CONCLUSION: Given the conservation of the functionally important residues and the ability to bind glutathione, YffB is likely to function as a GSH-dependent thiol reductase.
Crystal structure of the YffB protein from Pseudomonas aeruginosa suggests a glutathione-dependent thiol reductase function.,Teplyakov A, Pullalarevu S, Obmolova G, Doseeva V, Galkin A, Herzberg O, Dauter M, Dauter Z, Gilliland GL BMC Struct Biol. 2004 Mar 8;4:5. PMID:15102337[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
