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Crystal structures of three B-helical acetyltransferases
Reference
B09328
Principal Investigator / Supervisor
Professor Peter Moody
Co-Investigators /
Co-Supervisors
Institution
University of Leicester
Department
Biochemistry
Funding type
Research
Value (£)
137,190
Status
Completed
Type
Research Grant
Start date
11/09/1998
End date
11/09/2001
Duration
36 months
Abstract
NodL, SAT and XAT are three microbial O-acetyltransferases that share a common core of the recently identified trimer of left-handed beta-helices within their structures and have acetyl-CoA as the acyl donor and yet very different acyl acceptors. This core means the structures differ considerably from that of Chloramphicol Acetyl Transferase (CAT), which is also trimeric and has evolved to catalyse O-acetylation from the same donor. The determination of the crystal structures of these three enzymes will allow us to compare and contrast the structural similarities of the core of the molecule with the differing means of molecular recognition. All three enzymes have been crystallised and the structures of the enzymes with their substrates and co-factors will be determined.
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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