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Structural studies of AhrC the arginine-dependent repressor/activator from Bacillus subtilis

Reference	B06625
Principal Investigator / Supervisor	Professor Simon Phillips
Co-Investigators / Co-Supervisors	Dr Mark Parsons
Institution	University of Leeds
Department	Inst of Molecular & Cellular Biology
Funding type	Research
Value (£)	138,255
Status	Completed
Type	Research Grant
Start date	01/06/1997
End date	01/06/2000
Duration	36 months

Abstract

AhrC is a multifunctional, sequence-specific DNA-binding protein which acts as a transcriptional repressor, an activator and a factor in plasmid resolution. It is a hexameric protein which strongly bends DNA upon binding and has no strong sequence homology to other know DNA-binding proteins except Escherichia coli arginine repressor. We propose to determine the 3-dimensional structure of AhrC by X-ray crystallography in order to investigate the molecular basis of operator sequence specificity and of activation of DNA- binding by L-arginine. We have prepared and characterised crystals of apo-and holo-AhrC and also intend to crystallise and solve the structures of complexes of AhrC with operator DNA to probe the diverse functions of the protein.

Summary

unavailable

Committee	Closed Committee - Biomolecular Sciences (BMS)
Research Topics	X – not assigned to a current Research Topic
Research Priority	X – Research Priority information not available
Research Initiative	X - not in an Initiative
Funding Scheme	X – not Funded via a specific Funding Scheme

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