Crystal structure of the YffB protein fromPseudomonas aeruginosasuggests a glutathione-dependent thiol reductase function
✍ Scribed by Alexey Teplyakov; Sadhana Pullalarevu; Galina Obmolova; Victoria Doseeva; Andrey Galkin; Osnat Herzberg; Miroslawa Dauter; Zbigniew Dauter; Gary L Gilliland
- Publisher
- BioMed Central
- Year
- 2004
- Tongue
- English
- Weight
- 573 KB
- Volume
- 4
- Category
- Article
- ISSN
- 1472-6807
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✦ Synopsis
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.