6ppe: Difference between revisions
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New page: '''Unreleased structure''' The entry 6ppe is ON HOLD Authors: Description: Category: Unreleased Structures |
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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 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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.19Å</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> | |||
== Function == | |||
[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. | |||
==See Also== | |||
*[[Clp protease 3D structures|Clp protease 3D structures]] | |||
__TOC__ | |||
[[Category: | </StructureSection> | ||
[[Category: Escherichia coli]] | |||
[[Category: Large Structures]] | |||
[[Category: Fei X]] | |||
[[Category: Harrison SC]] | |||
[[Category: Jenni S]] | |||
[[Category: Sauer RT]] | |||
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
FunctionCLPP_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 |
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