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X-ray crystallography of DNA gyrase

Reference	BBS/E/J/0000X019
Principal Investigator / Supervisor	Professor Anthony Maxwell
Co-Investigators / Co-Supervisors
Institution	John Innes Centre
Department	John Innes Centre Department
Funding type	Research
Value (£)	10,351
Status	Completed
Type	Institute Project
Start date	01/04/2001
End date	31/03/2004
Duration	36 months

Abstract

DNA gyrase is a member of the class of enzymes known as the DNA topoisomerases, which are vital for a number of cellular processes including replication transcription and recombination. Gyrase is unique in that it is the only enzyme of the group that can actively introduce supercoils into DNA. It is an essential enzyme in bacteria but is absent from eukaryotes and as such is an ideal drug target. This lab works on a number of aspects of DNA gyrase and the related enzymes DNA topoisomerase II (from human cells) and DNA topoisomerase IV from bacteria. These include structure, mechanism of action and interaction with drugs. In recent years our structural efforts have been focused on x-ray crystallography and we have determined the structure of a number of protein domains and their complexes with drugs and ligands. A great deal of biochemical work has been based on these structures. An obvious goal of our current structural work is to determine the structure of the gyrase-DNA complex. This is an ambitious target that will depend on a number of factors. However, we have a number of other short-term targets that can probably be realised in the next 2-3 years. In addition, it is expected that the project will involve a fair amount of biochemistry/molecular biology, in terms of producing and characterising protein fragments and complexes.

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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