1ass: Difference between revisions

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New page: left|200px<br /><applet load="1ass" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ass, resolution 2.3Å" /> '''APICAL DOMAIN OF THE ...
 
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[[Image:1ass.gif|left|200px]]<br /><applet load="1ass" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1ass, resolution 2.3&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='1ass' size='340' side='right'caption='[[1ass]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ass]] 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=1ASS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ASS 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]] 2.3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <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=1ass FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ass OCA], [https://pdbe.org/1ass PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ass RCSB], [https://www.ebi.ac.uk/pdbsum/1ass PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ass 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/1ass_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=1ass ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1ASS 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 NA and PO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ASS OCA].
*[[Chaperonin 3D structures|Chaperonin 3D structures]]
 
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
==Reference==
__TOC__
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]
</StructureSection>
[[Category: Single protein]]
[[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: NA]]
[[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 11:06:39 2007''

Latest revision as of 09:33, 7 February 2024

APICAL DOMAIN OF THE CHAPERONIN FROM THERMOPLASMA ACIDOPHILUMAPICAL DOMAIN OF THE CHAPERONIN FROM THERMOPLASMA ACIDOPHILUM

Structural highlights

1ass is a 1 chain structure with sequence from Thermoplasma acidophilum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.3Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

THSA_THEAC Molecular chaperone; binds unfolded polypeptides in vitro, and has a weak ATPase activity.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1ass, resolution 2.30Å

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