6ppe: Difference between revisions

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<StructureSection load='6ppe' size='340' side='right'caption='[[6ppe]], [[Resolution|resolution]] 3.19&Aring;' scene=''>
<StructureSection load='6ppe' size='340' side='right'caption='[[6ppe]], [[Resolution|resolution]] 3.19&Aring;' scene=''>
== Structural highlights ==
== 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>
<table><tr><td colspan='2'>[[6ppe]] is a 28 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. 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 [https://proteopedia.org/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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.19&#8491;</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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6ppe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ppe OCA], [https://pdbe.org/6ppe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ppe RCSB], [https://www.ebi.ac.uk/pdbsum/6ppe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ppe ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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]
[https://www.uniprot.org/uniprot/CLPP_ECOLI CLPP_ECOLI] 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. May play the role of a master protease which is attracted to different substrates by different specificity factors such as ClpA or ClpX.
<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>
==See Also==
 
*[[Clp protease 3D structures|Clp protease 3D structures]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6ppe" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Endopeptidase Clp]]
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Fei, X]]
[[Category: Fei X]]
[[Category: Harrison, S C]]
[[Category: Harrison SC]]
[[Category: Jenni, S]]
[[Category: Jenni S]]
[[Category: Sauer, R T]]
[[Category: Sauer RT]]
[[Category: Aaa+ protease complex]]
[[Category: Chaperone]]
[[Category: Protein degradation]]

Latest revision as of 12:26, 20 March 2024

ClpP and ClpX IGF loop in ClpX-ClpP complex with D7 symmetryClpP and ClpX IGF loop in ClpX-ClpP complex with D7 symmetry

Structural highlights

6ppe is a 28 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Electron Microscopy, Resolution 3.19Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CLPP_ECOLI 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. May play the role of a master protease which is attracted to different substrates by different specificity factors such as ClpA or ClpX.

See Also

6ppe, resolution 3.19Å

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