6em9: Difference between revisions
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''' | {{Large structure}} | ||
==S.aureus ClpC resting state, asymmetric map== | |||
<StructureSection load='6em9' size='340' side='right' caption='[[6em9]], [[Resolution|resolution]] 8.40Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6em9]] is a 10 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EM9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6EM9 FirstGlance]. <br> | |||
</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=6em9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6em9 OCA], [http://pdbe.org/6em9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6em9 RCSB], [http://www.ebi.ac.uk/pdbsum/6em9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6em9 ProSAT]</span></td></tr> | |||
</table> | |||
{{Large structure}} | |||
== Function == | |||
[[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. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6em9" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bukau, B]] | [[Category: Bukau, B]] | ||
[[Category: Carroni, M]] | |||
[[Category: Franke, K]] | [[Category: Franke, K]] | ||
[[Category: Mogk, A]] | [[Category: Mogk, A]] | ||
[[Category: | [[Category: Aaa+ protease]] | ||
[[Category: Chaperone]] | |||
[[Category: Clpc]] | |||
[[Category: Oligomeric complex]] | |||
Revision as of 11:44, 27 December 2017
S.aureus ClpC resting state, asymmetric mapS.aureus ClpC resting state, asymmetric map
Structural highlights
Warning: this is a large structure, and loading might take a long time or not happen at all. Function[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. Publication Abstract from PubMedRing-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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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