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<StructureSection load='1ass' size='340' side='right'caption='[[1ass]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='1ass' size='340' side='right'caption='[[1ass]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1ass]] is a 1 chain structure. 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>
<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='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>
</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>
<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>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/THSA_THEAC THSA_THEAC]] Molecular chaperone; binds unfolded polypeptides in vitro, and has a weak ATPase activity.  
[https://www.uniprot.org/uniprot/THSA_THEAC THSA_THEAC] Molecular chaperone; binds unfolded polypeptides in vitro, and has a weak ATPase activity.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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/main_output.php?pdb_ID=1ass ConSurf].
</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>
<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.
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>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1ass" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Chaperonin 3D structures|Chaperonin 3D structures]]
*[[Chaperonin 3D structures|Chaperonin 3D structures]]
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Baumeister, W]]
[[Category: Essen, L O]]
[[Category: Klumpp, M]]
[[Category: Atp-binding]]
[[Category: Chaperonin]]
[[Category: Groel]]
[[Category: Hsp60]]
[[Category: Tcp1]]
[[Category: Thermoplasma acidophilum]]
[[Category: Thermoplasma acidophilum]]
[[Category: Thermosome]]
[[Category: Baumeister W]]
[[Category: Essen L-O]]
[[Category: Klumpp M]]

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