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

DOI: 10.1107/S1744309110053078 DOI Help
PMID: 21393832 PMID Help

Authors: Tung Le (University of East Anglia) , Clare Stevenson (John Innes Centre) , Mark Buttner (John Innes Centre) , David Lawson (John Innes Centre)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acta Crystallographica Section F Structural Biology And Crystallization Communications , VOL 67 (3) , PAGES 307-309

State: Published (Approved)
Published: February 2011

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.

Subject Areas: Biology and Bio-materials


Instruments: I03-Macromolecular Crystallography

Added On: 22/02/2011 14:10

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