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


CONCLUSIONS
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.
Teplyakov
Alexey
A
Center for Advanced Research in Biotechnology, University of Maryland Biotechnology Institute, 9600 Gudelsky Drive, Rockville, MD 20850, USA. teplyako@umbi.umd.edu
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
D053501:Arsenite Transporting ATPases; D001426:Bacterial Proteins / Q000737:chemistry*; D017124:Conserved Sequence; D018360:Crystallography, X-Ray; D016623:Ion Pumps / Q000737:chemistry; D008958:Models, Molecular; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009097:Multienzyme Complexes / Q000737:chemistry; D011490:Protein Disulfide Reductase (Glutathione) / Q000737:chemistry*; D017510:Protein Folding; D017434:Protein Structure, Tertiary / Q000502:physiology; D011550:Pseudomonas aeruginosa / Q000201:enzymology*; D017386:Sequence Homology, Amino Acid; D013329:Structure-Activity Relationship
D001426:Bacterial Proteins; D016623:Ion Pumps; D009097:Multienzyme Complexes; D011490:Protein Disulfide Reductase (Glutathione); D053501:Arsenite Transporting ATPases