|Title||Crystal structure of the YffB protein from Pseudomonas aeruginosa suggests a glutathione-dependent thiol reductase function.|
|Publication Type||Journal Article|
|Year of Publication||2004|
|Authors||Teplyakov, A, Pullalarevu, S, Obmolova, G, Doseeva, V, Galkin, A, Herzberg, O, Dauter, M, Dauter, Z, Gilliland, GL|
|Journal||BMC Struct Biol|
|Date Published||2004 Mar 8|
|Keywords||Arsenite 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|
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.
|Alternate Journal||BMC Struct. Biol.|
|PubMed Central ID||PMC387831|
|Grant List||P01-GM57890 / GM / NIGMS NIH HHS / United States|