Use this URL to cite or link to this record in EThOS: http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.504736
Title: Disentangling an unfoldase : structural studies of ClpB
Author: Wright, David
Awarding Body: Birkbeck (University of London)
Current Institution: Birkbeck (University of London)
Date of Award: 2008
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Abstract:
ClpB is a bacterial Hsp 100 chaperone that has been shown to cooperate with the DnaKfJ (Hsp70/40) chaperone system in the removal of aggregated protein from cells. The HsplOO chaperones are members of the AAA+ super-family with two AAA+ domains per monomer. These proteins in their biologically active state from ring like oligomers, which have proved very hard to study with crystallographic techniques. We have studied the biologically active oligomer of E. Coli ClpB in both nucleotide bound and apo states by using negative stain and cryo electron microscopy techniques. We used image analysis and single particle reconstruction teclmiques to obtain 3 dimensional reconstructions at intermediate resolution of the biological oligomer under both sets of conditions. This reveals E. Coli ClpB forms a two layered heptameric ring with a large cavity in the centre. These particles are asymmetric at resolutions better than ~ 20 A suggesting that ClpB follows sequential or random ATP turnover kinetics. _.' Fitting X-ray crystal structures to the ClpB reconstructions shows that ClpB undergoes large domain movements during its active cycle and provides support for a threading mechanism of unfolding and disaggregation.
Supervisor: Not available Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID: uk.bl.ethos.504736  DOI: Not available
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