1a6d

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[[Image:1a6d.png|left|200px]]
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==THERMOSOME FROM T. ACIDOPHILUM==
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<StructureSection load='1a6d' size='340' side='right' caption='[[1a6d]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1a6d]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermoplasma_acidophilum Thermoplasma acidophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A6D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1A6D FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1a6d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a6d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1a6d RCSB], [http://www.ebi.ac.uk/pdbsum/1a6d PDBsum]</span></td></tr>
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<table>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a6/1a6d_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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We have determined to 2.6 A resolution the crystal structure of the thermosome, the archaeal group II chaperonin from T. acidophilum. The hexadecameric homolog of the eukaryotic chaperonin CCT/TRiC shows an (alphabeta)4(alphabeta)4 subunit assembly. Domain folds are homologous to GroEL but form a novel type of inter-ring contact. The domain arrangement resembles the GroEL-GroES cis-ring. Parts of the apical domains form a lid creating a closed conformation. The lid substitutes for a GroES-like cochaperonin that is absent in the CCT/TRiC system. The central cavity has a polar surface implicated in protein folding. Binding of the transition state analog Mg-ADP-AIF3 suggests that the closed conformation corresponds to the ATP form.
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{{STRUCTURE_1a6d| PDB=1a6d | SCENE= }}
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Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT.,Ditzel L, Lowe J, Stock D, Stetter KO, Huber H, Huber R, Steinbacher S Cell. 1998 Apr 3;93(1):125-38. PMID:9546398<ref>PMID:9546398</ref>
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===THERMOSOME FROM T. ACIDOPHILUM===
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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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{{ABSTRACT_PUBMED_9546398}}
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==About this Structure==
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[[1a6d]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermoplasma_acidophilum Thermoplasma acidophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A6D OCA].
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==See Also==
==See Also==
*[[Chaperonin|Chaperonin]]
*[[Chaperonin|Chaperonin]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:009546398</ref><references group="xtra"/>
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__TOC__
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</StructureSection>
[[Category: Thermoplasma acidophilum]]
[[Category: Thermoplasma acidophilum]]
[[Category: Ditzel, L.]]
[[Category: Ditzel, L.]]

Revision as of 08:34, 23 July 2014

THERMOSOME FROM T. ACIDOPHILUM

1a6d, resolution 2.60Å

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