6pp8: Difference between revisions

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-'''Unreleased structure'''
-The entry 6pp8 is ON HOLD
+==ClpX in ClpX-ClpP complex bound to substrate and ATP-gamma-S, class 1==
+<StructureSection load='6pp8' size='340' side='right'caption='[[6pp8]], [[Resolution|resolution]] 4.12&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6pp8]] is a 7 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PP8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6PP8 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='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=6pp8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pp8 OCA], [http://pdbe.org/6pp8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6pp8 RCSB], [http://www.ebi.ac.uk/pdbsum/6pp8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6pp8 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/A0A1Q9L861_ECOLX A0A1Q9L861_ECOLX]] ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP.[HAMAP-Rule:MF_00175][SAAS:SAAS01076750]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+ClpXP is an ATP-dependent protease in which the ClpX AAA+ motor binds, unfolds, and translocates specific protein substrates into the degradation chamber of ClpP. We present cryo-EM studies of the E. coli enzyme that show how asymmetric hexameric rings of ClpX bind symmetric heptameric rings of ClpP and interact with protein substrates. Subunits in the ClpX hexamer assume a spiral conformation and interact with two-residue segments of substrate in the axial channel, as observed for other AAA+ proteases and protein-remodeling machines. Strictly sequential models of ATP hydrolysis and a power stroke that moves two residues of the substrate per translocation step have been inferred from these structural features for other AAA+ unfoldases, but biochemical and single-molecule biophysical studies indicate that ClpXP operates by a probabilistic mechanism in which five to eight residues are translocated for each ATP hydrolyzed. We propose structure-based models that could account for the functional results.
-Authors:
+Structures of the ATP-fueled ClpXP proteolytic machine bound to protein substrate.,Fei X, Bell TA, Jenni S, Stinson BM, Baker TA, Harrison SC, Sauer RT Elife. 2020 Feb 28;9. pii: 52774. doi: 10.7554/eLife.52774. PMID:32108573<ref>PMID:32108573</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6pp8" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Fei, X]]
+[[Category: Harrison, S C]]
+[[Category: Jenni, S]]
+[[Category: Sauer, R T]]
+[[Category: Aaa+ protease complex]]
+[[Category: Chaperone]]
+[[Category: Protein degradation]]