6emw

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m (Protected "6emw" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 6emw is ON HOLD
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==Structure of S.aureus ClpC in complex with MecA==
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<StructureSection load='6emw' size='340' side='right' caption='[[6emw]], [[Resolution|resolution]] 11.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6emw]] is a 42 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EMW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6EMW FirstGlance]. <br>
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6emw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6emw OCA], [http://pdbe.org/6emw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6emw RCSB], [http://www.ebi.ac.uk/pdbsum/6emw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6emw ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/CLPC_STAAB CLPC_STAAB]] Required for growth at high temperatures, probably by acting as a chaperone during heat shock and targeting heat-denatured proteins for degradation by ClpP. [[http://www.uniprot.org/uniprot/A0A077UK83_STAAU A0A077UK83_STAAU]] Enables the recognition and targeting of unfolded and aggregated proteins to the ClpC protease or to other proteins involved in proteolysis.[HAMAP-Rule:MF_01124][SAAS:SAAS00950444]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Ring-forming AAA+ chaperones exert ATP-fueled substrate unfolding by threading through a central pore. This activity is potentially harmful requiring mechanisms for tight repression and substrate-specific activation. The AAA+ chaperone ClpC with the peptidase ClpP forms a bacterial protease essential to virulence and stress resistance. The adaptor MecA activates ClpC by targeting substrates and stimulating ClpC ATPase activity. We show how ClpC is repressed in its ground state by determining ClpC cryo-EM structures with and without MecA. ClpC forms large two-helical assemblies that associate via head-to-head contacts between coiled-coil middle domains (MDs). MecA converts this resting state to an active planar ring structure by binding to MD interaction sites. Loss of ClpC repression in MD mutants causes constitutive activation and severe cellular toxicity. These findings unravel an unexpected regulatory concept executed by coiled-coil MDs to tightly control AAA+ chaperone activity.
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Authors: Carroni, M., Mogk, A., Bukau, B., Franke, K.
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Regulatory coiled-coil domains promote head-to-head assemblies of AAA+ chaperones essential for tunable activity control.,Carroni M, Franke KB, Maurer M, Jager J, Hantke I, Gloge F, Linder D, Gremer S, Turgay K, Bukau B, Mogk A Elife. 2017 Nov 22;6. doi: 10.7554/eLife.30120. PMID:29165246<ref>PMID:29165246</ref>
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Description: Structure of S.aureus ClpC in complex with MecA
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 6emw" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Bukau, B]]
[[Category: Bukau, B]]
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[[Category: Carroni, M]]
[[Category: Franke, K]]
[[Category: Franke, K]]
[[Category: Mogk, A]]
[[Category: Mogk, A]]
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[[Category: Carroni, M]]
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[[Category: Aaa+ protein]]
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[[Category: Chaperone]]
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[[Category: Unfoldase]]

Revision as of 08:42, 27 December 2017

Structure of S.aureus ClpC in complex with MecA

6emw, resolution 11.00Å

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