Award details

The high resolution structure of domain III of proton-translocating nicotinamide nucleotide transhydrogenase

Reference	SBD07558
Principal Investigator / Supervisor	Professor Baz Jackson
Co-Investigators / Co-Supervisors	Dr Kevin Smith, Dr Scott Andrew White
Institution	University of Birmingham
Department	Sch of Geography, Earth & Env Sciences
Funding type	Research
Value (£)	145,952
Status	Completed
Type	Research Grant
Start date	13/10/1997
End date	13/10/2000
Duration	36 months

Abstract

Transhydrogenase pumps protons across a membrane. Domain III of the protein probably contains the essential machinery that couples the chemical reaction (hydride transfer between NAD(H) and NADP(H) to H+ translocation. We have expressed and purified domain III protein from bacterial transhydrogenase in large quantities. The recombinant protein has a very high affinity for NADP(H) and, together with the ND(H)-binding domain I protein, can catalyse hydride transfer, even in the absence of the membrane-intercalating domain II. Recombinant domain III protein of transhydrogenase is soluble and stable; it has an excellent 1H- 1H 2D NMR spectrum. The primary objective of this work is to solve the high-resolution structure of the protein using NMR spectroscopy. We shall also initiate crystallisation trials of the domain I:III complex with a view to obtaining high resolution structure by X-ray diffraction.

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	Structural biology and design applications (SBD) [1996]
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