3j02

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<SX load='3j02' size='340' side='right' viewer='molstar' caption='[[3j02]], [[Resolution|resolution]] 8.00&Aring;' scene=''>
<SX load='3j02' size='340' side='right' viewer='molstar' caption='[[3j02]], [[Resolution|resolution]] 8.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3j02]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43000 Atcc 43000]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J02 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3J02 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3j02]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanococcus_maripaludis Methanococcus maripaludis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J02 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3J02 FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3j03|3j03]]</div></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&#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=3j02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j02 OCA], [https://pdbe.org/3j02 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3j02 RCSB], [https://www.ebi.ac.uk/pdbsum/3j02 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3j02 ProSAT]</span></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=3j02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j02 OCA], [https://pdbe.org/3j02 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3j02 RCSB], [https://www.ebi.ac.uk/pdbsum/3j02 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3j02 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/Q877G8_METMI Q877G8_METMI]
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Chaperonins are large ATP-driven molecular machines that mediate cellular protein folding. Group II chaperonins use their "built-in lid" to close their central folding chamber. Here we report the structure of an archaeal group II chaperonin in its prehydrolysis ATP-bound state at subnanometer resolution using single particle cryo-electron microscopy (cryo-EM). Structural comparison of Mm-cpn in ATP-free, ATP-bound, and ATP-hydrolysis states reveals that ATP binding alone causes the chaperonin to close slightly with a approximately 45 degrees counterclockwise rotation of the apical domain. The subsequent ATP hydrolysis drives each subunit to rock toward the folding chamber and to close the lid completely. These motions are attributable to the local interactions of specific active site residues with the nucleotide, the tight couplings between the apical and intermediate domains within the subunit, and the aligned interactions between two subunits across the rings. This mechanism of structural changes in response to ATP is entirely different from those found in group I chaperonins.
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Cryo-EM structure of a group II chaperonin in the prehydrolysis ATP-bound state leading to lid closure.,Zhang J, Ma B, DiMaio F, Douglas NR, Joachimiak LA, Baker D, Frydman J, Levitt M, Chiu W Structure. 2011 May 11;19(5):633-9. PMID:21565698<ref>PMID:21565698</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 3j02" 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__
</SX>
</SX>
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[[Category: Atcc 43000]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Baker, D]]
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[[Category: Methanococcus maripaludis]]
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[[Category: Chiu, W]]
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[[Category: Baker D]]
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[[Category: DiMaio, F]]
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[[Category: Chiu W]]
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[[Category: Douglas, N R]]
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[[Category: DiMaio F]]
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[[Category: Frydman, J]]
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[[Category: Douglas NR]]
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[[Category: Joachimiak, L]]
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[[Category: Frydman J]]
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[[Category: Levitt, M]]
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[[Category: Joachimiak L]]
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[[Category: Ma, B]]
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[[Category: Levitt M]]
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[[Category: Zhang, J]]
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[[Category: Ma B]]
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[[Category: Atp-bound]]
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[[Category: Zhang J]]
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[[Category: Chaperone]]
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[[Category: Chaperonin]]
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[[Category: Mm-cpn]]
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Current revision

Lidless D386A Mm-cpn in the pre-hydrolysis ATP-bound state

3j02, resolution 8.00Å

Proteopedia Page Contributors and Editors (what is this?)

OCA

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