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Structural insight into the oxidation-sensing mechanism of the antibiotic resistance of regulator MexR.

ABSTRACT: MexR 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.

SUBMITTER: Chen H

PROVIDER: S-EPMC2933878 | biostudies-literature | 2010 Sep

REPOSITORIES: biostudies-literature

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Structural insight into the oxidation-sensing mechanism of the antibiotic resistance of regulator MexR.

Chen Hao H Yi Chengqi C Zhang Jin J Zhang Wenru W Ge Zhiyun Z Yang Cai-Guang CG He Chuan C

EMBO reports 20100709 9

MexR 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 ...[more]

PMID: 20616806

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