6rn3

From Proteopedia

(Difference between revisions)

Revision as of 05:46, 11 April 2020

ClpB (DWB mutant) bound to casein in presence of ATPgammaS - state WT-2A

6rn3, resolution 4.00Å

Structural highlights

6rn3 is a 7 chain structure with sequence from Bovin and Escherichia coli hvh 50 (4-2593475). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	6qs4, 6qs6, 6qs7, 6qs8, 6rn2
Gene:	clpB, G723_01503 (Escherichia coli HVH 50 (4-2593475))
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Deville C, Franke K, Mogk A, Bukau B, Saibil HR. Two-Step Activation Mechanism of the ClpB Disaggregase for Sequential Substrate Threading by the Main ATPase Motor. Cell Rep. 2019 Jun 18;27(12):3433-3446.e4. doi: 10.1016/j.celrep.2019.05.075. PMID:31216466 doi:http://dx.doi.org/10.1016/j.celrep.2019.05.075

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6rn3"

@@ Line 3: / Line 3: @@
 <SX load='6rn3' size='340' side='right' viewer='molstar' caption='[[6rn3]], [[Resolution|resolution]] 4.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6rn3]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin] and [http://en.wikipedia.org/wiki/Escherichia_coli_hvh_50_(4-2593475) Escherichia coli hvh 50 (4-2593475)]. 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>
+<table><tr><td colspan='2'>[[6rn3]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin] and [http://en.wikipedia.org/wiki/Escherichia_coli_hvh_50_(4-2593475) Escherichia coli hvh 50 (4-2593475)]. 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://proteopedia.org/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>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">clpB, G723_01503 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280998 Escherichia coli HVH 50 (4-2593475)])</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>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/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 ==

6rn3

From Proteopedia

Revision as of 05:46, 11 April 2020

ClpB (DWB mutant) bound to casein in presence of ATPgammaS - state WT-2A

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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