3mex
From Proteopedia
Crystal structure of MexR in oxidized state
Structural highlights
FunctionMEXR_PSEAE Repressor of the mexAB-oprM multidrug resistance operon. Also represses its own expression. Many variants lead to increased expression of the mexAB-oprM operon. 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 PubMedMexR functions as the primary regulator of the mexAB-oprM multidrug efflux expression in Pseudomonas aeruginosa. It has been shown that MexR senses oxidative stress by interprotomer disulphide bond formation between redox-active cysteines. This oxidation induces MexR to dissociate from the promoter DNA, thus activating the transcriptional expression of efflux pump genes. In this study, we present the crystal structure of MexR in its oxidized form at a resolution of 2.1 A. This crystal structure reveals the mechanism by which oxidative signal allosterically derepresses the MexR-controlled transcription activation. Structural insight into the oxidation-sensing mechanism of the antibiotic resistance of regulator MexR.,Chen H, Yi C, Zhang J, Zhang W, Ge Z, Yang CG, He C EMBO Rep. 2010 Sep;11(9):685-90. Epub 2010 Jul 9. PMID:20616806[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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Categories: Large Structures | Pseudomonas aeruginosa PAO1 | Chen H | He C | Yang C-G | Yi C | Zhang J | Zhang W
