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Abstract Background The <it>yffB </it>(PA3664) gene of <it>Pseudomonas aeruginosa </it>encodes an uncharacterized protein of 13 kDa molecular weight with a marginal sequence similarity to arsenate reductase from <it>Escherichia coli</it>. 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 Å 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.</p

Crystal structure of the YffB protein from Pseudomonas aeruginosa suggests a glutathione-dependent thiol reductase function.