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| | <StructureSection load='1e0r' size='340' side='right'caption='[[1e0r]], [[Resolution|resolution]] 2.80Å' scene=''> | | <StructureSection load='1e0r' size='340' side='right'caption='[[1e0r]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1e0r]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"thermoplasma_acidophila"_(sic)_darland_et_al._1970 "thermoplasma acidophila" (sic) darland et al. 1970]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E0R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E0R FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1e0r]] 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=1E0R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E0R FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ass|1ass]], [[1asx|1asx]], [[1a6d|1a6d]], [[1a6e|1a6e]]</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]] 2.8Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1e0r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e0r OCA], [http://pdbe.org/1e0r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1e0r RCSB], [http://www.ebi.ac.uk/pdbsum/1e0r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1e0r 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=1e0r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e0r OCA], [https://pdbe.org/1e0r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e0r RCSB], [https://www.ebi.ac.uk/pdbsum/1e0r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e0r ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/THSB_THEAC THSB_THEAC]] Molecular chaperone; binds unfolded polypeptides in vitro, and has a weak ATPase activity. | + | [https://www.uniprot.org/uniprot/THSB_THEAC THSB_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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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Baumeister, W]] | |
| - | [[Category: Bosch, G]] | |
| - | [[Category: Essen, L O]] | |
| - | [[Category: Chaperonin]] | |
| - | [[Category: Groel]] | |
| - | [[Category: Hsp60]] | |
| - | [[Category: Tcp1]] | |
| | [[Category: Thermoplasma acidophilum]] | | [[Category: Thermoplasma acidophilum]] |
| - | [[Category: Thermosome]] | + | [[Category: Baumeister W]] |
| | + | [[Category: Bosch G]] |
| | + | [[Category: Essen L-O]] |
| Structural highlights
Function
THSB_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.
Publication Abstract from PubMed
The crystal structure of the beta-apical domain of the thermosome, an archaeal group II chaperonin from Thermoplasma acidophilum, has been determined at 2.8 A resolution. The structure shows an invariant globular core from which a 25 A long protrusion emanates, composed of an elongated alpha-helix (H10) and a long extended stretch consisting of residues GluB245-ThrB253. A comparison with previous apical domain structures reveals a large segmental displacement of the protruding part of helix H10 via the hinge GluB276-ValB278. The region comprising residues GluB245-ThrB253 adopts an extended beta-like conformation rather than the alpha-helix seen in the alpha-apical domain. Consequently, it appears that the protrusions of the apical domains from group II chaperonins might assume a variety of context-dependent conformations during an open, substrate-accepting state of the chaperonin. Sequence variations in the protrusion regions that are found in the eukaryotic TRiC/CCT subunits may provide different structural propensities and hence serve different roles in substrate recognition.
Crystal structure of the beta-apical domain of the thermosome reveals structural plasticity in the protrusion region.,Bosch G, Baumeister W, Essen LO J Mol Biol. 2000 Aug 4;301(1):19-25. PMID:10926489[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Bosch G, Baumeister W, Essen LO. Crystal structure of the beta-apical domain of the thermosome reveals structural plasticity in the protrusion region. J Mol Biol. 2000 Aug 4;301(1):19-25. PMID:10926489 doi:10.1006/jmbi.2000.3955
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