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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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