View source for 7eko


==CrClpP-S1==
<StructureSection load='7eko' size='340' side='right'caption='[[7eko]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7eko]] is a 15 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlamydomonas_reinhardtii Chlamydomonas reinhardtii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7EKO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7EKO 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]] 3.3&#8491;</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=7eko FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7eko OCA], [https://pdbe.org/7eko PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7eko RCSB], [https://www.ebi.ac.uk/pdbsum/7eko PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7eko ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A8IJ60_CHLRE A8IJ60_CHLRE] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Protein homoeostasis in plastids is strategically regulated by the protein quality control system involving multiple chaperones and proteases, among them the Clp protease. Here, we determined the structure of the chloroplast ClpP complex from Chlamydomonas reinhardtii by cryo-electron microscopy. ClpP contains two heptameric catalytic rings without any symmetry. The top ring contains one ClpR6, three ClpP4 and three ClpP5 subunits while the bottom ring is composed of three ClpP1(C) subunits and one each of the ClpR1-4 subunits. ClpR3, ClpR4 and ClpT4 subunits connect the two rings and stabilize the complex. The chloroplast Cpn11/20/23 co-chaperonin, a co-factor of Cpn60, forms a cap on the top of ClpP by protruding mobile loops into hydrophobic clefts at the surface of the top ring. The co-chaperonin repressed ClpP proteolytic activity in vitro. By regulating Cpn60 chaperone and ClpP protease activity, the co-chaperonin may play a role in coordinating protein folding and degradation in the chloroplast.

The cryo-EM structure of the chloroplast ClpP complex.,Wang N, Wang Y, Zhao Q, Zhang X, Peng C, Zhang W, Liu Y, Vallon O, Schroda M, Cong Y, Liu C Nat Plants. 2021 Nov;7(11):1505-1515. doi: 10.1038/s41477-021-01020-x. Epub 2021 , Nov 15. PMID:34782772<ref>PMID:34782772</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7eko" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Chlamydomonas reinhardtii]]
[[Category: Large Structures]]
[[Category: Cong Y]]
[[Category: Liu CM]]
[[Category: Wang N]]
[[Category: Wang YF]]