Structural highlights
Function
OHRB_BACSU Involved in organic hydroperoxide resistance.[1]
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
The crystal structure of the fully oxidized form of the Bacillus subtilis organic hydroperoxide-resistance (OhrB) protein is reported at 2.1 A resolution. The electron density reveals an intact catalytic disulfide bond (Cys55-Cys119) in each of the two molecules, which are intertwined into a canonical obligate dimer. However, the stereochemistry of the disulfides is unorthodox and strained, suggesting that they are sensitive to reducing agents. A deep solvent-accessible gorge reaching Cys55 may represent the access route for the reductant.
Structure of the Bacillus subtilis OhrB hydroperoxide-resistance protein in a fully oxidized state.,Cooper DR, Surendranath Y, Devedjiev Y, Bielnicki J, Derewenda ZS Acta Crystallogr D Biol Crystallogr. 2007 Dec;63(Pt 12):1269-73. Epub 2007, Nov 16. PMID:18084074[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Fuangthong M, Atichartpongkul S, Mongkolsuk S, Helmann JD. OhrR is a repressor of ohrA, a key organic hydroperoxide resistance determinant in Bacillus subtilis. J Bacteriol. 2001 Jul;183(14):4134-41. PMID:11418552 doi:http://dx.doi.org/10.1128/JB.183.14.4134-4141.2001
- ↑ Cooper DR, Surendranath Y, Devedjiev Y, Bielnicki J, Derewenda ZS. Structure of the Bacillus subtilis OhrB hydroperoxide-resistance protein in a fully oxidized state. Acta Crystallogr D Biol Crystallogr. 2007 Dec;63(Pt 12):1269-73. Epub 2007, Nov 16. PMID:18084074 doi:10.1107/S0907444907050226
