3wvl

<StructureSection load='3wvl' size='340' side='right'caption='[[3wvl]], [[Resolution|resolution]] 3.79&Aring;' scene=''>

<table><tr><td colspan='2'>[[3wvl]] is a 28 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WVL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WVL FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=3wvl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wvl OCA], [https://pdbe.org/3wvl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wvl RCSB], [https://www.ebi.ac.uk/pdbsum/3wvl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wvl ProSAT]</span></td></tr>

== Function ==

[[https://www.uniprot.org/uniprot/CH60_ECOLI CH60_ECOLI]] Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.[HAMAP-Rule:MF_00600] Essential for the growth of the bacteria and the assembly of several bacteriophages. Also plays a role in coupling between replication of the F plasmid and cell division of the cell.[HAMAP-Rule:MF_00600] [[https://www.uniprot.org/uniprot/CH10_ECOLI CH10_ECOLI]] Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.[HAMAP-Rule:MF_00580]

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== Publication Abstract from PubMed ==

The chaperonin GroEL is an essential chaperone that assists in protein folding with the aid of GroES and ATP. GroEL forms a double-ring structure, and both rings can bind GroES in the presence of ATP. Recent progress on the GroEL mechanism has revealed the importance of a symmetric 1:2 GroEL:GroES2 complex (the "football"-shaped complex) as a critical intermediate during the functional GroEL cycle. We determined the crystal structure of the football GroEL:GroES2-ATP14 complex from Escherichia coli at 3.8A, using a GroEL mutant that is extremely defective in ATP hydrolysis. The overall structure of the football complex resembled the GroES-bound GroEL ring of the asymmetric 1:1 GroEL:GroES complex (the "bullet" complex). However, the two GroES-bound GroEL rings form a modified interface by an ~7 degrees rotation about the 7-fold axis. As a result, the inter-ring contacts between the two GroEL rings in the football complex differed from those in the bullet complex. The differences provide a structural basis for the apparently impaired inter-ring negative cooperativity observed in several biochemical analyses.

Crystal structure of a symmetric football-shaped GroEL:GroES2-ATP14 complex determined at 3.8A reveals rearrangement between two GroEL rings.,Koike-Takeshita A, Arakawa T, Taguchi H, Shimamura T J Mol Biol. 2014 Oct 23;426(21):3634-41. doi: 10.1016/j.jmb.2014.08.017. Epub, 2014 Aug 28. PMID:25174333<ref>PMID:25174333</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 3wvl" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Chaperonin ATPase]]

[[Category: Arakawa, T]]

[[Category: Koike-Takeshita, A]]

[[Category: Shimamura, T]]

[[Category: Taguchi, H]]

[[Category: Protein folding]]