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Structural and functional analysis of ammonium transport proteins

Reference	BBS/E/J/0000A164
Principal Investigator / Supervisor	Professor Mike Merrick
Co-Investigators / Co-Supervisors
Institution	John Innes Centre
Department	John Innes Centre Department
Funding type	Research
Value (£)	57,438
Status	Completed
Type	Institute Project
Start date	19/01/2004
End date	18/01/2007
Duration	36 months

Abstract

The Amt family of high-affinity ammonium transport proteins is conserved in bacteria, plants and animals, and includes the human Rhesus proteins. We have developed the Escherichia coli AmtB protein as a model for this family. It can be purified to homogeneity and preliminary experiments have given 2D crystals that diffract to 9Å. The objectives of the project are: (1) to produce high-resolution 2D and 3D structures of Amt proteins, and of an AmtB-GlnK complex by electron microscopy or X-ray crystallography; (2) to use mutagenesis of AmtB to identify specific residues involved in ammonium binding and transport and thereby to elucidate structure/function relationships in the protein; (3) to develop an in vitro system in order to investigate the mode of action of AmtB.

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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