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Structural studies on V-ATPase from Thermus thermophilus
Reference
BBS/B/06458
Principal Investigator / Supervisor
Professor So Iwata
Co-Investigators /
Co-Supervisors
Institution
Imperial College London
Department
Biological Sciences
Funding type
Research
Value (£)
239,774
Status
Completed
Type
Research Grant
Start date
01/04/2004
End date
31/12/2007
Duration
45 months
Abstract
The V-Type ATPases (V-ATPase) reside within many intracellular compartments and function in processes such as receptor-mediated endocytosis and protein processing and degradation. V-ATPases have also been identified in the plasma membrane of certain cells where they are important in acid secretion and bone degradation. In spite of the importance for these cell functions, very little is known about the structure of V-ATPase. The V-ATPase from Thermus thermophilus is ideal for structural studies because of its stability; we have already obtained the crystals of the whole complex and various subunits. The main objective of this proposal is to determine the complete structure of V-ATPase and to deduce the coupling mechanism of proton translocation and ATP hydrolysis / synthesis.
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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