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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)