1ass
From Proteopedia
(Difference between revisions)
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<StructureSection load='1ass' size='340' side='right'caption='[[1ass]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='1ass' size='340' side='right'caption='[[1ass]], [[Resolution|resolution]] 2.30Å' 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]] 2.3Å</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. | |
== 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. | ||
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| - | 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®/PubMed®, 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: | + | [[Category: Baumeister W]] |
| + | [[Category: Essen L-O]] | ||
| + | [[Category: Klumpp M]] | ||
Current revision
APICAL DOMAIN OF THE CHAPERONIN FROM THERMOPLASMA ACIDOPHILUM
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