6em9: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 6em9 is ON HOLD
+==S.aureus ClpC resting state, asymmetric map==
+<SX load='6em9' size='340' side='right' viewer='molstar' caption='[[6em9]], [[Resolution|resolution]] 8.40&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6em9]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Staab Staab]. 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://proteopedia.org/fgij/fg.htm?mol=6EM9 FirstGlance]. <br>
+</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">clpC, SAB0475 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=273036 STAAB])</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/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>
+== 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.
-Authors: Carroni, M., Mogk, A., Bukau, B., Franke, K.
+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>
-Description: S.aureus ClpC resting state, asymmetric map
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6em9" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</SX>
+[[Category: Large Structures]]
+[[Category: Staab]]
 [[Category: Bukau, B]]
+[[Category: Carroni, M]]
 [[Category: Franke, K]]
 [[Category: Mogk, A]]
-[[Category: Carroni, M]]
+[[Category: Aaa+ protease]]
+[[Category: Chaperone]]
+[[Category: Clpc]]
+[[Category: Oligomeric complex]]