1rw1

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YFFB (PA3664) PROTEINYFFB (PA3664) PROTEIN

Structural highlights

1rw1 is a 1 chain structure with sequence from Pseudomonas aeruginosa PAO1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.02Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q9HXX5_PSEAE

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

Crystal structure of the YffB protein from Pseudomonas aeruginosa suggests a glutathione-dependent thiol reductase function.,Teplyakov A, Pullalarevu S, Obmolova G, Doseeva V, Galkin A, Herzberg O, Dauter M, Dauter Z, Gilliland GL BMC Struct Biol. 2004 Mar 8;4:5. PMID:15102337[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Teplyakov A, Pullalarevu S, Obmolova G, Doseeva V, Galkin A, Herzberg O, Dauter M, Dauter Z, Gilliland GL. Crystal structure of the YffB protein from Pseudomonas aeruginosa suggests a glutathione-dependent thiol reductase function. BMC Struct Biol. 2004 Mar 8;4:5. PMID:15102337 doi:10.1186/1472-6807-4-5

1rw1, resolution 1.02Å

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OCA