Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 2004 Mar 8:4:5.
doi: 10.1186/1472-6807-4-5.

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

Alexey Teplyakov  1 , Sadhana Pullalarevu, Galina Obmolova, Victoria Doseeva, Andrey Galkin, Osnat Herzberg, Miroslawa Dauter, Zbigniew Dauter, Gary L Gilliland
Affiliations

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

Alexey Teplyakov et al. BMC Struct Biol. .

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.

PubMed Disclaimer

Figures

Figure 1
Figure 1
(Left) Ribbon presentation of the polypeptide fold of YffB. Active site residues are shown as ball-and-stick models (produced with MOLSCRIPT [19]). (Right) Electrostatic surface potential calculated with GRASP [20]. Positive charges are blue and negative are red.
See this image and copyright information in PMC

References

    1. Bateman A, Birney E, Durbin R, Eddy SR, Howe KL, Sonnhammer EL. The Pfam protein families database. Nucleic Acids Res. 2000;28:263–266. doi: 10.1093/nar/28.1.263. - DOI - PMC - PubMed
    1. Mukhopadhyay R, Rosen BP, Phung le T, Silver S. Microbial arsenic: from geocycles to genes and enzymes. FEMS Microbiol Rev. 2002;26:311–325. doi: 10.1016/S0168-6445(02)00112-2. - DOI - PubMed
    1. Gladysheva TB, Oden KL, Rosen BP. Properties of the arsenate reductase of plasmid R773. Biochemistry. 1994;33:7288–7293. doi: 10.1021/bi00189a033. - DOI - PubMed
    1. Martin P, DeMel S, Shi J, Gladysheva T, Gatti DL, Rosen BP, Edwards BF. Insights into the structure, solvation, and mechanism of ArsC arsenate reductase, a novel arsenic detoxification enzyme. Structure. 2001;9:1071–1081. doi: 10.1016/S0969-2126(01)00672-4. - DOI - PubMed
    1. Ji G, Garber EA, Armes LG, Chen CM, Fuchs JA, Silver S. Arsenate reductase of Staphylococcus aureus plasmid pI258. Biochemistry. 1994;33:7294–7299. doi: 10.1021/bi00189a034. - DOI - PubMed

Publication types

MeSH terms

Associated data

LinkOut - more resources