6ppe: Difference between revisions
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==ClpP and ClpX IGF loop in ClpX-ClpP complex with D7 symmetry== | |||
<StructureSection load='6ppe' size='340' side='right'caption='[[6ppe]], [[Resolution|resolution]] 3.19Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6ppe]] is a 28 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PPE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6PPE FirstGlance]. <br> | |||
</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Endopeptidase_Clp Endopeptidase Clp], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.92 3.4.21.92] </span></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=6ppe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ppe OCA], [http://pdbe.org/6ppe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ppe RCSB], [http://www.ebi.ac.uk/pdbsum/6ppe PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ppe ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/A0A0K4NM46_ECOLX A0A0K4NM46_ECOLX]] Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.[HAMAP-Rule:MF_00444][RuleBase:RU000550][SAAS:SAAS00674840] [[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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6ppe" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Endopeptidase Clp]] | |||
[[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]] | |||