6rn3: Difference between revisions
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==ClpB (DWB mutant) bound to casein in presence of ATPgammaS - state WT-2A== | |||
<StructureSection load='6rn3' size='340' side='right'caption='[[6rn3]], [[Resolution|resolution]] 4.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6rn3]] is a 7 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RN3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6RN3 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</scene></td></tr> | |||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6qs4|6qs4]], [[6qs6|6qs6]], [[6qs7|6qs7]], [[6qs8|6qs8]], [[6rn2|6rn2]]</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=6rn3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rn3 OCA], [http://pdbe.org/6rn3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rn3 RCSB], [http://www.ebi.ac.uk/pdbsum/6rn3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rn3 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/V2RJ62_ECOLX V2RJ62_ECOLX]] Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE.[RuleBase:RU362034] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
AAA+ proteins form asymmetric hexameric rings that hydrolyze ATP and thread substrate proteins through a central channel via mobile substrate-binding pore loops. Understanding how ATPase and threading activities are regulated and intertwined is key to understanding the AAA+ protein mechanism. We studied the disaggregase ClpB, which contains tandem ATPase domains (AAA1, AAA2) and shifts between low and high ATPase and threading activities. Coiled-coil M-domains repress ClpB activity by encircling the AAA1 ring. Here, we determine the mechanism of ClpB activation by comparing ATPase mechanisms and cryo-EM structures of ClpB wild-type and a constitutively active ClpB M-domain mutant. We show that ClpB activation reduces ATPase cooperativity and induces a sequential mode of ATP hydrolysis in the AAA2 ring, the main ATPase motor. AAA1 and AAA2 rings do not work synchronously but in alternating cycles. This ensures high grip, enabling substrate threading via a processive, rope-climbing mechanism. | |||
Two-Step Activation Mechanism of the ClpB Disaggregase for Sequential Substrate Threading by the Main ATPase Motor.,Deville C, Franke K, Mogk A, Bukau B, Saibil HR Cell Rep. 2019 Jun 18;27(12):3433-3446.e4. doi: 10.1016/j.celrep.2019.05.075. PMID:31216466<ref>PMID:31216466</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6rn3" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Deville, C]] | [[Category: Deville, C]] | ||
[[Category: Saibil, H R]] | |||
[[Category: Aaa]] | |||
[[Category: Chaperone]] | |||
[[Category: Disaggregase]] | |||
[[Category: Proteostasis]] | |||
Revision as of 09:10, 3 July 2019
ClpB (DWB mutant) bound to casein in presence of ATPgammaS - state WT-2AClpB (DWB mutant) bound to casein in presence of ATPgammaS - state WT-2A
Structural highlights
Function[V2RJ62_ECOLX] Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE.[RuleBase:RU362034] Publication Abstract from PubMedAAA+ proteins form asymmetric hexameric rings that hydrolyze ATP and thread substrate proteins through a central channel via mobile substrate-binding pore loops. Understanding how ATPase and threading activities are regulated and intertwined is key to understanding the AAA+ protein mechanism. We studied the disaggregase ClpB, which contains tandem ATPase domains (AAA1, AAA2) and shifts between low and high ATPase and threading activities. Coiled-coil M-domains repress ClpB activity by encircling the AAA1 ring. Here, we determine the mechanism of ClpB activation by comparing ATPase mechanisms and cryo-EM structures of ClpB wild-type and a constitutively active ClpB M-domain mutant. We show that ClpB activation reduces ATPase cooperativity and induces a sequential mode of ATP hydrolysis in the AAA2 ring, the main ATPase motor. AAA1 and AAA2 rings do not work synchronously but in alternating cycles. This ensures high grip, enabling substrate threading via a processive, rope-climbing mechanism. Two-Step Activation Mechanism of the ClpB Disaggregase for Sequential Substrate Threading by the Main ATPase Motor.,Deville C, Franke K, Mogk A, Bukau B, Saibil HR Cell Rep. 2019 Jun 18;27(12):3433-3446.e4. doi: 10.1016/j.celrep.2019.05.075. PMID:31216466[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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