Award details

Molecular recognition and the transmission of conformational change in bacterial HisGs

Reference	BBS/B/06814
Principal Investigator / Supervisor	Dr Adrian Lapthorn
Co-Investigators / Co-Supervisors
Institution	University of Glasgow
Department	School of Chemistry
Funding type	Research
Value (£)	191,100
Status	Completed
Type	Research Grant
Start date	01/05/2004
End date	30/04/2007
Duration	36 months

Abstract

ATP phosphoribosyl transferase (HisG) is the highly regulated first enzyme of the histidine biosynthetic pathway. Two distinct forms of the enzyme exist, the long form that is active as a dimer and forms inactive hexamers, and a short form that is inactive unless complexed with HisZ in a hetero octamer. We propose to structurally characterise the molecular basis of enzyme activity and inhibition by AMP and histidine in these divergent forms of the same enzyme. We have solved the structure of a long form HisG and shown by mutagenesis that a truncated pseudo short form of this enzyme is active. In addition we have shown that natural short forms of HisG in the absence of HisZ can be activated by temperature. A combination of molecular biology and biophysical techniques will be used to extend our understanding of how the flexibility and hence activity are controlled by aggregation.

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

I accept the terms and conditions of use (opens in new window)

export PDF file

back to list new search