Structural analysis of non-native protein binding to chaperonin complexes. (360G-Wellcome-079604_Z_06_Z)
The research project is aimed at understanding the mechanism of assisted protein folding by chaperonins. The GroEL-GroES molecular chaperone system is required in almost all cells for the correct folding of a subset of essential cellular proteins. It is known that non-native proteins bind to the cavity surface of GroEL and then become encapsulated in a folding chamber by a process that leads to their release from the initial binding sites. There is little known about conformational changes of the substrate protein during its interaction with GroEL. The approach of cryo EM and image processing provides unique information on the structures of chaperonin-substrate complexes, since it is one of the only structural biology methods that can provide 3-dimensional structures from heterogeneous populations. Structures of complexes with substrates such as METK, the tetrameric enzyme S-adenosyl methionine synthetase, that stringently requires GroE for its folding, will provide new insights into the details of chaperonin-substrate interaction, including the 3D density distribution of a natural substrate and its interaction sites on GroEL. The single particle analysis and separation methods are well established in the Birkbeck laboratory, and the project will provide high level training in cryo EM and image processing for the applicant.
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Grant Details
Amount Awarded | 271475 |
Applicant Surname | Natesh |
Approval Committee | Basic Science Interview Committee |
Award Date | 2006-06-29T00:00:00+00:00 |
Financial Year | 2005/06 |
Grant Programme: Title | Intermediate Fellowship: Inactive scheme |
Internal ID | 079604/Z/06/Z |
Lead Applicant | Dr Ramanathan Natesh |
Partnership Value | 271475 |
Planned Dates: End Date | 2010-08-15T00:00:00+00:00 |
Planned Dates: Start Date | 2007-04-16T00:00:00+00:00 |
Recipient Org: Country | United Kingdom |
Region | Greater London |
Sponsor(s) | Prof Helen Saibil |