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

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TitleCrystal structure of the YffB protein from Pseudomonas aeruginosa suggests a glutathione-dependent thiol reductase function.
Publication TypeJournal Article
Year of Publication2004
AuthorsTeplyakov, A, Pullalarevu, S, Obmolova, G, Doseeva, V, Galkin, A, Herzberg, O, Dauter, M, Dauter, Z, Gilliland, GL
JournalBMC Struct Biol
Volume4
Pagination5
Date Published2004 Mar 8
ISSN1472-6807
KeywordsArsenite Transporting ATPases, Bacterial Proteins, Conserved Sequence, Crystallography, X-Ray, Ion Pumps, Models, Molecular, Molecular Sequence Data, Molecular Weight, Multienzyme Complexes, Protein Disulfide Reductase (Glutathione), Protein Folding, Protein Structure, Tertiary, Pseudomonas aeruginosa, Sequence Homology, Amino Acid, Structure-Activity Relationship
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.

DOI10.1186/1472-6807-4-5
Alternate JournalBMC Struct. Biol.
PubMed ID15102337
PubMed Central IDPMC387831
Grant ListP01-GM57890 / GM / NIGMS NIH HHS / United States