1a6e: Difference between revisions

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New page: left|200px<br /> <applet load="1a6e" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a6e, resolution 3.2Å" /> '''THERMOSOME-MG-ADP-AL...
 
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[[Image:1a6e.gif|left|200px]]<br />
<applet load="1a6e" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1a6e, resolution 3.2&Aring;" />
'''THERMOSOME-MG-ADP-ALF3 COMPLEX'''<br />


==Overview==
==THERMOSOME-MG-ADP-ALF3 COMPLEX==
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.
<StructureSection load='1a6e' size='340' side='right'caption='[[1a6e]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1a6e]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermoplasma_acidophilum Thermoplasma acidophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A6E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A6E FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=AF3:ALUMINUM+FLUORIDE'>AF3</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=1a6e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a6e OCA], [https://pdbe.org/1a6e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a6e RCSB], [https://www.ebi.ac.uk/pdbsum/1a6e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a6e ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/THSA_THEAC THSA_THEAC] Molecular chaperone; binds unfolded polypeptides in vitro, and has a weak ATPase activity.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a6/1a6e_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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/main_output.php?pdb_ID=1a6e ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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.


==About this Structure==
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>
1A6E is a [[http://en.wikipedia.org/wiki/Protein_complex Protein complex]] structure of sequences from [[http://en.wikipedia.org/wiki/Thermoplasma_acidophilum Thermoplasma acidophilum]] with MG, ADP and AF3 as [[http://en.wikipedia.org/wiki/ligands ligands]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1A6E OCA]].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9546398 9546398]
</div>
[[Category: Protein complex]]
<div class="pdbe-citations 1a6e" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Chaperonin 3D structures|Chaperonin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thermoplasma acidophilum]]
[[Category: Thermoplasma acidophilum]]
[[Category: Ditzel, L.]]
[[Category: Ditzel L]]
[[Category: Huber, H.]]
[[Category: Huber H]]
[[Category: Huber, R.]]
[[Category: Huber R]]
[[Category: Loewe, J.]]
[[Category: Loewe J]]
[[Category: Steinbacher, S.]]
[[Category: Steinbacher S]]
[[Category: Stetter, K.O.]]
[[Category: Stetter K-O]]
[[Category: Stock, D.]]
[[Category: Stock D]]
[[Category: ADP]]
[[Category: AF3]]
[[Category: MG]]
[[Category: atp hydrolysis]]
[[Category: atpase]]
[[Category: cct]]
[[Category: group ii chaperonin]]
[[Category: protein folding]]
[[Category: thermoplasma acidophilum]]
[[Category: transition state complex]]
[[Category: tric]]
 
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