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

DOI: 10.1107/S1744309110053078
PMID: 21393832

Authors: Tung B. K. Le (University of East Anglia) , Clare E. M. Stevenson (John Innes Centre) , Mark J. Buttner (John Innes Centre) , David M. 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.

Journal Keywords: TetR-like repressors; simocyclinone; efflux pumps; antibiotic resistance

Subject Areas: Biology and Bio-materials, Medicine


Instruments: I03-Macromolecular Crystallography

Added On: 22/02/2011 14:10

Discipline Tags:

Pathogens Antibiotic Resistance Infectious Diseases Health & Wellbeing Structural biology Life Sciences & Biotech

Technical Tags:

Diffraction Macromolecular Crystallography (MX)