Research article

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

Alexey Teplyakov¹ , Sadhana Pullalarevu¹ , Galina Obmolova¹ , Victoria Doseeva¹ , Andrey Galkin¹ , Osnat Herzberg¹ , Miroslawa Dauter² , Zbigniew Dauter² and Gary L Gilliland¹

¹  Center for Advanced Research in Biotechnology, University of Maryland Biotechnology Institute and the National Institute of Standards and Technology, 9600 Gudelsky Drive, Rockville, MD 20850, U.S.A

²  National Cancer Institute, Brookhaven National Laboratory, Building 725A-X9, Upton, NY 11973, U.S.A

author email corresponding author email

BMC Structural Biology 2004, 4:5doi:10.1186/1472-6807-4-5

Published:	8 March 2004

Abstract

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 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.