1a6d

<StructureSection load='1a6d' size='340' side='right' caption='[[1a6d]], [[Resolution|resolution]] 2.60&Aring;' scene=''>

<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>

</td></tr><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=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>

[[http://www.uniprot.org/uniprot/THSA_THEAC THSA_THEAC]] Molecular chaperone; binds unfolded polypeptides in vitro, and has a weak ATPase activity. [[http://www.uniprot.org/uniprot/THSB_THEAC THSB_THEAC]] Molecular chaperone; binds unfolded polypeptides in vitro, and has a weak ATPase activity.

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a6/1a6d_consurf.spt"</scriptWhenChecked>

</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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== Publication Abstract from PubMed ==

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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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*[[Chaperonin|Chaperonin]]

[[Category: Ditzel, L]]

[[Category: Huber, H]]

[[Category: Huber, R]]

[[Category: Loewe, J]]

[[Category: Steinbacher, S]]

[[Category: Stetter, K O]]

[[Category: Stock, D]]

[[Category: Tric]]