1QVR: Crystal Structure Analysis of Clpb

Citation:
Abstract
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.
PDB ID: 1QVRDownload
MMDB ID: 25107
PDB Deposition Date: 2003/8/28
Updated in MMDB: 2007/11 
Experimental Method:
x-ray diffraction
Resolution: 3  Å
Source Organism:
Similar Structures:
Biological Unit for 1QVR: trimeric; determined by author and by software (PISA)
Molecular Components in 1QVR
Label Count Molecule
Proteins (3 molecules)
3
Clpb Protein
Molecule annotation
Chemicals (29 molecules)
1
23
2
6
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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