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New page: left|200px<br /><applet load="1asx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1asx, resolution 2.8Å" /> '''APICAL DOMAIN OF THE ...
 
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[[Image:1asx.gif|left|200px]]<br /><applet load="1asx" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1asx, resolution 2.8&Aring;" />
'''APICAL DOMAIN OF THE CHAPERONIN FROM THERMOPLASMA ACIDOPHILUM'''<br />


==Overview==
==APICAL DOMAIN OF THE CHAPERONIN FROM THERMOPLASMA ACIDOPHILUM==
The crystal structure of the substrate binding domain of the thermosome, the archaeal group II chaperonin, has been determined at 2.3 A resolution., The core resembles the apical domain of GroEL but lacks the hydrophobic, residues implied in binding of substrates to group I chaperonins. Rather, a large hydrophobic surface patch is found in a novel helix-turn-helix, motif, which is characteristic of all group II chaperonins including the, eukaryotic TRiC/CCT complex. Models of the holochaperonin, which are, consistent with cryo electron microscopy data, suggest a dual role of this, helical protrusion in substrate binding and controlling access to the, central cavity independent of a GroES-like cochaperonin.
<StructureSection load='1asx' size='340' side='right'caption='[[1asx]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1asx]] is a 1 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=1ASX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ASX 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]] 2.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=1asx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1asx OCA], [https://pdbe.org/1asx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1asx RCSB], [https://www.ebi.ac.uk/pdbsum/1asx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1asx 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/as/1asx_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1asx ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystal structure of the substrate binding domain of the thermosome, the archaeal group II chaperonin, has been determined at 2.3 A resolution. The core resembles the apical domain of GroEL but lacks the hydrophobic residues implied in binding of substrates to group I chaperonins. Rather, a large hydrophobic surface patch is found in a novel helix-turn-helix motif, which is characteristic of all group II chaperonins including the eukaryotic TRiC/CCT complex. Models of the holochaperonin, which are consistent with cryo electron microscopy data, suggest a dual role of this helical protrusion in substrate binding and controlling access to the central cavity independent of a GroES-like cochaperonin.


==About this Structure==
Structure of the substrate binding domain of the thermosome, an archaeal group II chaperonin.,Klumpp M, Baumeister W, Essen LO Cell. 1997 Oct 17;91(2):263-70. PMID:9346243<ref>PMID:9346243</ref>
1ASX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermoplasma_acidophilum Thermoplasma acidophilum] with PO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ASX OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Structure of the substrate binding domain of the thermosome, an archaeal group II chaperonin., Klumpp M, Baumeister W, Essen LO, Cell. 1997 Oct 17;91(2):263-70. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9346243 9346243]
</div>
[[Category: Single protein]]
<div class="pdbe-citations 1asx" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Chaperonin 3D structures|Chaperonin 3D structures]]
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thermoplasma acidophilum]]
[[Category: Thermoplasma acidophilum]]
[[Category: Baumeister, W.]]
[[Category: Baumeister W]]
[[Category: Essen, L.O.]]
[[Category: Essen L-O]]
[[Category: Klumpp, M.]]
[[Category: Klumpp M]]
[[Category: PO4]]
[[Category: atp-binding]]
[[Category: chaperonin]]
[[Category: groel]]
[[Category: hsp60]]
[[Category: tcp1]]
[[Category: thermoplasma acidophilum]]
[[Category: thermosome]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:06:56 2007''

Latest revision as of 10:55, 2 August 2023

APICAL DOMAIN OF THE CHAPERONIN FROM THERMOPLASMA ACIDOPHILUM

1asx, resolution 2.80Å

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