3j1e

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<SX load='3j1e' size='340' side='right' viewer='molstar' caption='[[3j1e]], [[Resolution|resolution]] 8.30&Aring;' scene=''>
<SX load='3j1e' size='340' side='right' viewer='molstar' caption='[[3j1e]], [[Resolution|resolution]] 8.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3j1e]] is a 18 chain structure with sequence from [http://en.wikipedia.org/wiki/"acidianus_tengchongenses"_he_et_al._2001 "acidianus tengchongenses" he et al. 2001]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J1E OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3J1E FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3j1e]] is a 18 chain structure with sequence from [https://en.wikipedia.org/wiki/Acidianus_tengchongensis Acidianus tengchongensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J1E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3J1E FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3j1b|3j1b]], [[3j1c|3j1c]], [[3j1d|3j1d]], [[3j1f|3j1f]], [[3j1g|3j1g]], [[3j1h|3j1h]], [[3j1i|3j1i]], [[3j1j|3j1j]], [[3j1k|3j1k]], [[3j1l|3j1l]]</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 8.3&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3j1e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j1e OCA], [http://pdbe.org/3j1e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3j1e RCSB], [http://www.ebi.ac.uk/pdbsum/3j1e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3j1e ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3j1e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j1e OCA], [https://pdbe.org/3j1e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3j1e RCSB], [https://www.ebi.ac.uk/pdbsum/3j1e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3j1e ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q877H2_9CREN Q877H2_9CREN]
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Group II chaperonins, which assemble as double-ring complexes, assist in the refolding of nascent peptides or denatured proteins in an ATP-dependent manner. The molecular mechanism of group II chaperonin assembly and thermal stability is yet to be elucidated. Here, we selected the group II chaperonins (cpn-alpha and cpn-beta), also called thermosomes, from Acidianus tengchongensis and investigated their assembly and thermal stability. We found that the binding of ATP or its analogs contributed to the successful assembly of thermosomes and enhanced their thermal stabilities. Cpn-beta is more thermally stable than cpn-alpha, while the thermal stability of the hetero thermosome cpn-alphabeta is intermediate. Cryo-electron microscopy reconstructions of cpn-alpha and cpn-beta revealed the interwoven densities of their non-conserved flexible N/C-termini around the equatorial planes. The deletion or swapping of their termini and pH-dependent thermal stability assays revealed the key role of the termini electrostatic interactions in the assembly and thermal stability of the thermosomes.
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Flexible interwoven termini determine the thermal stability of thermosomes.,Zhang K, Wang L, Liu Y, Chan KY, Pang X, Schulten K, Dong Z, Sun F Protein Cell. 2013 Jun;4(6):432-44. doi: 10.1007/s13238-013-3026-9. Epub 2013 May, 25. PMID:23709365<ref>PMID:23709365</ref>
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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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<div class="pdbe-citations 3j1e" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Chaperonin 3D structures|Chaperonin 3D structures]]
*[[Chaperonin 3D structures|Chaperonin 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
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[[Category: Acidianus tengchongenses he et al. 2001]]
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[[Category: Acidianus tengchongensis]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Chan, K Y]]
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[[Category: Chan KY]]
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[[Category: Dong, Z Y]]
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[[Category: Dong ZY]]
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[[Category: Gao, B]]
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[[Category: Gao B]]
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[[Category: Hu, Z J]]
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[[Category: Hu ZJ]]
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[[Category: Ji, G]]
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[[Category: Ji G]]
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[[Category: Liu, Y X]]
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[[Category: Liu YX]]
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[[Category: Schulten, K]]
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[[Category: Schulten K]]
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[[Category: Sun, F]]
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[[Category: Sun F]]
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[[Category: Wang, L]]
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[[Category: Wang L]]
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[[Category: Wang, X]]
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[[Category: Wang X]]
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[[Category: Zhang, K]]
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[[Category: Zhang K]]
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[[Category: Chaperone]]
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[[Category: Group ii chaperonin]]
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Current revision

Cryo-EM structure of 9-fold symmetric rATcpn-beta in apo state

3j1e, resolution 8.30Å

Proteopedia Page Contributors and Editors (what is this?)

OCA

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