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

Teplyakov, Alexey; Pullalarevu, Sadhana; Obmolova, Galina; Doseeva, Victoria; Galkin, Andrey; Herzberg, Osnat; Dauter, Miroslawa; Dauter, Zbigniew; Gilliland, Gary L.
January 2004
BMC Structural Biology;2004, Vol. 4, p1
Academic Journal
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 Ã… 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.


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