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

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 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.

SUBMITTER: Teplyakov A

PROVIDER: S-EPMC387831 | biostudies-literature | 2004 Mar

REPOSITORIES: biostudies-literature

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

Teplyakov Alexey A Pullalarevu Sadhana S Obmolova Galina G Doseeva Victoria V Galkin Andrey A Herzberg Osnat O Dauter Miroslawa M Dauter Zbigniew Z Gilliland Gary L GL

BMC structural biology 20040308

<h4>Background</h4>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.<h4>Results</h4>The structure was determined at 1.0 A resolution by single-wavelength anomalous diffraction. The fold is very ...[more]

PMID: 15102337

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