3kfb: Difference between revisions
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==Crystal structure of a group II chaperonin from Methanococcus maripaludis== | ==Crystal structure of a group II chaperonin from Methanococcus maripaludis== | ||
<StructureSection load='3kfb' size='340' side='right' caption='[[3kfb]], [[Resolution|resolution]] 3.20Å' scene=''> | <StructureSection load='3kfb' size='340' side='right'caption='[[3kfb]], [[Resolution|resolution]] 3.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3kfb]] is a 8 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3kfb]] is a 8 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=3KFB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KFB FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.2Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</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=3kfb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kfb OCA], [https://pdbe.org/3kfb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3kfb RCSB], [https://www.ebi.ac.uk/pdbsum/3kfb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3kfb ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q877G8_METMI Q877G8_METMI] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kf/3kfb_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kf/3kfb_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
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==See Also== | ==See Also== | ||
*[[Chaperonin|Chaperonin]] | *[[Chaperonin 3D structures|Chaperonin 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Adams | [[Category: Methanococcus maripaludis]] | ||
[[Category: Douglas | [[Category: Adams PD]] | ||
[[Category: Frydman | [[Category: Douglas N]] | ||
[[Category: Goulet | [[Category: Frydman J]] | ||
[[Category: King | [[Category: Goulet DR]] | ||
[[Category: Knee | [[Category: King JA]] | ||
[[Category: Meyer | [[Category: Knee KM]] | ||
[[Category: Pereira | [[Category: Meyer D]] | ||
[[Category: Ralston | [[Category: Pereira JH]] | ||
[[Category: Ralston CY]] | |||
Latest revision as of 05:01, 21 November 2024
Crystal structure of a group II chaperonin from Methanococcus maripaludisCrystal structure of a group II chaperonin from Methanococcus maripaludis
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedChaperonins are large protein complexes consisting of two stacked multisubunit rings, which open and close in an ATP-dependent manner to create a protected environment for protein folding. Here, we describe the first crystal structure of a group II chaperonin in an open conformation. We have obtained structures of the archaeal chaperonin from Methanococcus maripaludis in both a peptide acceptor (open) state and a protein folding (closed) state. In contrast with group I chaperonins, in which the equatorial domains share a similar conformation between the open and closed states and the largest motions occurs at the intermediate and apical domains, the three domains of the archaeal chaperonin subunit reorient as a single rigid body. The large rotation observed from the open state to the closed state results in a 65% decrease of the folding chamber volume and creates a highly hydrophilic surface inside the cage. These results suggest a completely distinct closing mechanism in the group II chaperonins as compared with the group I chaperonins. Crystal structures of a group II chaperonin reveal the open and closed states associated with the protein folding cycle.,Pereira JH, Ralston CY, Douglas NR, Meyer D, Knee KM, Goulet DR, King JA, Frydman J, Adams PD J Biol Chem. 2010 Sep 3;285(36):27958-66. Epub 2010 Jun 23. PMID:20573955[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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