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Crystallization and preliminary X-ray analysis of the TetR-like efflux pump regulator SimR.

ABSTRACT: Crystals of SimR were grown by vapour diffusion. The protein crystallized with trigonal symmetry and X-ray data were recorded to a resolution of 2.3?Å from a single crystal at the synchrotron. SimR belongs to the TetR family of bacterial transcriptional regulators. In the absence of the antibiotic simocyclinone, SimR represses the transcription of a divergently transcribed gene encoding the simocyclinone efflux pump SimX in Streptomyces antibioticus by binding to operators in the simR-simX intergenic region. Simocyclinone binding causes SimR to dissociate from its operators, leading to expression of the SimX efflux pump. Thus, SimR represents an intimate link between the biosynthesis of simocyclinone and its export, which may also provide the mechanism of self-resistance to the antibiotic in the producer strain.

SUBMITTER: Le TB

PROVIDER: S-EPMC3053152 | biostudies-literature | 2011 Mar

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray analysis of the TetR-like efflux pump regulator SimR.

Le Tung B K TB Stevenson Clare E M CE Buttner Mark J MJ Lawson David M DM

Acta crystallographica. Section F, Structural biology and crystallization communications 20110218 Pt 3

Crystals of SimR were grown by vapour diffusion. The protein crystallized with trigonal symmetry and X-ray data were recorded to a resolution of 2.3 Å from a single crystal at the synchrotron. SimR belongs to the TetR family of bacterial transcriptional regulators. In the absence of the antibiotic simocyclinone, SimR represses the transcription of a divergently transcribed gene encoding the simocyclinone efflux pump SimX in Streptomyces antibioticus by binding to operators in the simR-simX inter ...[more]

PMID: 21393832

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