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| [[Image:1qvr.gif|left|200px]] | | [[Image:1qvr.gif|left|200px]] |
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| {{STRUCTURE_1qvr| PDB=1qvr | SCENE= }} | | {{STRUCTURE_1qvr| PDB=1qvr | SCENE= }} |
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| '''Crystal Structure Analysis of ClpB'''
| | ===Crystal Structure Analysis of ClpB=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_14567920}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 14567920 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_14567920}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Aaa atpase]] | | [[Category: Aaa atpase]] |
| [[Category: Coiled coil]] | | [[Category: Coiled coil]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:45:23 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 18:03:17 2008'' |
