1qvr
From Proteopedia
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Crystal Structure Analysis of ClpB
Overview
Molecular chaperones assist protein folding by facilitating their, "forward" folding and preventing aggregation. However, once aggregates, have formed, these chaperones cannot facilitate protein disaggregation., Bacterial ClpB and its eukaryotic homolog Hsp104 are essential proteins of, the heat-shock response, which have the remarkable capacity to rescue, stress-damaged proteins from an aggregated state. We have determined the, structure of Thermus thermophilus ClpB (TClpB) using a combination of, X-ray crystallography and cryo-electron microscopy (cryo-EM). Our, single-particle reconstruction shows that TClpB forms a two-tiered, hexameric ring. The ClpB/Hsp104-linker consists of an 85 A long and mobile, coiled coil that is located on the outside of the hexamer. Our mutagenesis, and biochemical data show that both the relative position and motion of, this coiled coil are critical for chaperone function. Taken together, we, propose a mechanism by which an ATP-driven conformational change is, coupled to a large coiled-coil motion, which is indispensable for protein, disaggregation.
About this Structure
1QVR is a Single protein structure of sequence from Thermus thermophilus with PT and ANP as ligands. Full crystallographic information is available from OCA.
Reference
The structure of ClpB: a molecular chaperone that rescues proteins from an aggregated state., Lee S, Sowa ME, Watanabe YH, Sigler PB, Chiu W, Yoshida M, Tsai FT, Cell. 2003 Oct 17;115(2):229-40. PMID:14567920
Page seeded by OCA on Wed Nov 21 01:02:23 2007
Categories: Single protein | Thermus thermophilus | Chiu, W. | Lee, S. | Sigler, P.B. | Sowa, M.E. | Tsai, F.T.F. | Watanabe, Y. | Yoshida, M. | ANP | PT | Aaa atpase | Coiled coil
