This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
6ppe
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 6ppe is ON HOLD Authors: Description: Category: Unreleased Structures) |
|||
| (3 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==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]] | ||
Current revision
ClpP and ClpX IGF loop in ClpX-ClpP complex with D7 symmetry
| |||||||||||
