Conformational stability of the full-atom hexameric model of the ClpB chaperone from Escherichia coli
The Escherichia coli heat shock protein ClpB, a member of the Hsp100 family, plays a crucial role in cellular thermotolerance. In co‐operation with the Hsp70 chaperone system, it is able to solubilize proteins aggregated by heat shock conditions and refold them into the native state in an ATP‐depend...
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Published in | Biopolymers Vol. 93; no. 1; pp. 47 - 60 |
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Main Authors | , , , , |
Format | Journal Article |
Language | English |
Published |
Hoboken
Wiley Subscription Services, Inc., A Wiley Company
01.01.2010
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Subjects | |
Online Access | Get full text |
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Summary: | The Escherichia coli heat shock protein ClpB, a member of the Hsp100 family, plays a crucial role in cellular thermotolerance. In co‐operation with the Hsp70 chaperone system, it is able to solubilize proteins aggregated by heat shock conditions and refold them into the native state in an ATP‐dependent way. It was established that the mechanism of ClpB action depends on the formation of a ring‐shaped hexameric structure and the translocation of a protein substrate through an axial channel. The structural aspects of this process are not fully known. By means of homology modeling and protein–protein docking, we obtained a model of the hexameric arrangement of the full‐length ClpB protein complexed with ATP. A molecular dynamics simulation of this model was performed to assess its flexibility and conformational stability. The high mobility of the “linker” M‐domain, essential for the renaturing activity of ClpB, was demonstrated, and the size and shape of central channel were analyzed. In this model, we propose the coordinates for a loop between b4 and B6 structural elements, not defined in previous structural research, which faces the inside of the channel and may therefore play a role in substrate translocation. © 2009 Wiley Periodicals, Inc. Biopolymers 93: 47–60, 2010.
This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com |
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Bibliography: | State Committee for Scientific Research - No. DS 8372-4-0138-9 Baker Laboratory of Chemistry and Chemical Biology ark:/67375/WNG-ZW97RQVT-W Polish Ministry of Science and Higher Education - No. N301 04631/1515 Informatics Center of the Metropolitan Academic Network (IC MAN) in Gdańsk Foundation for Polish Science ArticleID:BIP21294 Cornell University istex:F6A55D1ADED60B097990149542BAB0E1B6A04C5A ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 ObjectType-Article-2 ObjectType-Feature-1 |
ISSN: | 0006-3525 1097-0282 |
DOI: | 10.1002/bip.21294 |