5x9v: Difference between revisions

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'''Unreleased structure'''


The entry 5x9v is ON HOLD  until Paper Publication
==Crystal structure of group III chaperonin in the Closed state==
<StructureSection load='5x9v' size='340' side='right' caption='[[5x9v]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5x9v]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X9V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5X9V FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5x9u|5x9u]]</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=5x9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x9v OCA], [http://pdbe.org/5x9v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5x9v RCSB], [http://www.ebi.ac.uk/pdbsum/5x9v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5x9v ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The chaperonins (CPNs) are megadalton sized hollow complexes with two cavities that open and close to encapsulate non-native proteins. CPNs are assigned to two sequence-related groups that have distinct allosteric mechanisms. In Group I CPNs a detachable co-chaperone, GroES, closes the chambers whereas in Group II a built-in lid closes the chambers. Group I CPNs have a bacterial ancestry, whereas Group II CPNs are archaeal in origin. Here we describe open and closed crystal structures representing a new phylogenetic branch of CPNs. These Group III CPNs are divergent in sequence and structure from extant CPNs, but are closed by a built-in lid like Group II CPNs. A nucleotide-sensing loop, present in both Group I and Group II CPNs, is notably absent. We identified inter-ring pivot joints that articulate during ring closure. These Group III CPNs likely represent a relic from the ancestral CPN that formed distinct bacterial and archaeal branches.Chaperonins (CPNs) are ATP-dependent protein-folding machines. Here the authors present the open and closed crystal structures of a Group III CPN from the thermophilic bacterium Carboxydothermus hydrogenoformans, discuss its mechanism and structurally compare it with Group I and II CPNs.


Authors: An, Y.J., Cha, S.S.
Structural and mechanistic characterization of an archaeal-like chaperonin from a thermophilic bacterium.,An YJ, Rowland SE, Na JH, Spigolon D, Hong SK, Yoon YJ, Lee JH, Robb FT, Cha SS Nat Commun. 2017 Oct 10;8(1):827. doi: 10.1038/s41467-017-00980-z. PMID:29018216<ref>PMID:29018216</ref>


Description: Crystal structure of group III chaperonin in the Closed state
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Cha, S.S]]
<div class="pdbe-citations 5x9v" style="background-color:#fffaf0;"></div>
[[Category: An, Y.J]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: An, Y J]]
[[Category: Cha, S S]]
[[Category: Ancestral cpn60]]
[[Category: Archaeal-like bacterial chaperonin]]
[[Category: Chaperone]]
[[Category: Closed state]]
[[Category: Group iii]]
[[Category: Pivot joint]]
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