5cdi

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'''Unreleased structure'''
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{{Large structure}}
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==Chloroplast chaperonin 60b1 of Chlamydomonas==
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<StructureSection load='5cdi' size='340' side='right' caption='[[5cdi]], [[Resolution|resolution]] 3.81&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5cdi]] is a 14 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CDI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CDI FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5cdj|5cdj]], [[5cdk|5cdk]]</td></tr>
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<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=5cdi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cdi OCA], [http://pdbe.org/5cdi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cdi RCSB], [http://www.ebi.ac.uk/pdbsum/5cdi PDBsum]</span></td></tr>
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</table>
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{{Large structure}}
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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BACKGROUND: Chloroplast chaperonin, consisting of multiple subunits, mediates folding of the highly abundant protein Rubisco with the assistance of co-chaperonins. ATP hydrolysis drives the chaperonin allosteric cycle to assist substrate folding and promotes disassembly of chloroplast chaperonin. The ways in which the subunits cooperate during this cycle remain unclear. RESULTS: Here, we report the first crystal structure of Chlamydomonas chloroplast chaperonin homo-oligomer (CPN60beta1) at 3.8 A, which shares structural topology with typical type I chaperonins but with looser compaction, and possesses a larger central cavity, less contact sites and an enlarged ATP binding pocket compared to GroEL. The overall structure of Cpn60 resembles the GroEL allosteric intermediate state. Moreover, two amino acid (aa) residues (G153, G154) conserved among Cpn60s are involved in ATPase activity regulated by co-chaperonins. Domain swapping analysis revealed that the monomeric state of CPN60alpha is controlled by its equatorial domain. Furthermore, the C-terminal segment (aa 484-547) of CPN60beta influenced oligomer disassembly and allosteric rearrangement driven by ATP hydrolysis. The entire equatorial domain and at least one part of the intermediate domain from CPN60alpha are indispensable for functional cooperation with CPN60beta1, and this functional cooperation is strictly dependent on a conserved aa residue (E461) in the CPN60alpha subunit. CONCLUSIONS: The first crystal structure of Chlamydomonas chloroplast chaperonin homo-oligomer (CPN60beta1) is reported. The equatorial domain maintained the monomeric state of CPN60alpha and the C-terminus of CPN60beta affected oligomer disassembly driven by ATP. The cooperative roles of CPN60 subunits were also established.
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The entry 5cdi is ON HOLD until Paper Publication
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Structural insight into the cooperation of chloroplast chaperonin subunits.,Zhang S, Zhou H, Yu F, Bai C, Zhao Q, He J, Liu C BMC Biol. 2016 Apr 12;14:29. doi: 10.1186/s12915-016-0251-8. PMID:27072913<ref>PMID:27072913</ref>
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Authors: Zhang, S., Zhou, H., Yu, F., Gao, F., He, J., Liu, C.
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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Description: Chloroplast chaperonin 60b1 of Chlamydomonas
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<div class="pdbe-citations 5cdi" style="background-color:#fffaf0;"></div>
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[[Category: Unreleased Structures]]
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== References ==
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[[Category: Zhou, H]]
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<references/>
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[[Category: Zhang, S]]
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__TOC__
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</StructureSection>
[[Category: Gao, F]]
[[Category: Gao, F]]
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[[Category: He, J]]
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[[Category: Liu, C]]
[[Category: Yu, F]]
[[Category: Yu, F]]
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[[Category: Liu, C]]
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[[Category: Zhang, S]]
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[[Category: He, J]]
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[[Category: Zhou, H]]
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[[Category: Chaperone]]
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[[Category: Chaperonin complex]]

Revision as of 16:53, 15 May 2016

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Chloroplast chaperonin 60b1 of Chlamydomonas

5cdi, resolution 3.81Å

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