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| | <StructureSection load='4xci' size='340' side='right'caption='[[4xci]], [[Resolution|resolution]] 3.00Å' scene=''> | | <StructureSection load='4xci' size='340' side='right'caption='[[4xci]], [[Resolution|resolution]] 3.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4xci]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Sacs2 Sacs2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XCI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XCI FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4xci]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus_P2 Saccharolobus solfataricus P2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XCI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XCI FirstGlance]. <br> |
| - | </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=4xci FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xci OCA], [http://pdbe.org/4xci PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xci RCSB], [http://www.ebi.ac.uk/pdbsum/4xci PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4xci ProSAT]</span></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]] 3.0023Å</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=4xci FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xci OCA], [https://pdbe.org/4xci PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xci RCSB], [https://www.ebi.ac.uk/pdbsum/4xci PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xci ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/THSB_SULSO THSB_SULSO]] Molecular chaperone; binds unfolded polypeptides in vitro, and has a weak ATPase activity. [[http://www.uniprot.org/uniprot/THSA_SULSO THSA_SULSO]] Molecular chaperone; binds unfolded polypeptides in vitro, and has a weak ATPase activity. | + | [https://www.uniprot.org/uniprot/THSB_SACS2 THSB_SACS2] Molecular chaperone; binds unfolded polypeptides in vitro, and has a weak ATPase activity. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Sacs2]] | + | [[Category: Saccharolobus solfataricus P2]] |
| - | [[Category: Chaston, J J]] | + | [[Category: Chaston JJ]] |
| - | [[Category: Smits, C]] | + | [[Category: Smits C]] |
| - | [[Category: Stewart, A G]] | + | [[Category: Stewart AG]] |
| - | [[Category: Stock, D]] | + | [[Category: Stock D]] |
| - | [[Category: Chaperone]]
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| - | [[Category: Chaperonin]]
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| - | [[Category: Protein folding]]
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| - | [[Category: Thermosome]]
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| Structural highlights
Function
THSB_SACS2 Molecular chaperone; binds unfolded polypeptides in vitro, and has a weak ATPase activity.
Publication Abstract from PubMed
Chaperonins are essential biological complexes assisting protein folding in all kingdoms of life. Whereas homooligomeric bacterial GroEL binds hydrophobic substrates non-specifically, the heterooligomeric eukaryotic CCT binds specifically to distinct classes of substrates. Sulfolobales, which survive in a wide range of temperatures, have evolved three different chaperonin subunits (alpha, beta, gamma) that form three distinct complexes tailored for different substrate classes at cold, normal, and elevated temperatures. The larger octadecameric beta complexes cater for substrates under heat stress, whereas smaller hexadecameric alphabeta complexes prevail under normal conditions. The cold-shock complex contains all three subunits, consistent with greater substrate specificity. Structural analysis using crystallography and electron microscopy reveals the geometry of these complexes and shows a novel arrangement of the alpha and beta subunits in the hexadecamer enabling incorporation of the gamma subunit.
Structural and Functional Insights into the Evolution and Stress Adaptation of Type II Chaperonins.,Chaston JJ, Smits C, Aragao D, Wong AS, Ahsan B, Sandin S, Molugu SK, Molugu SK, Bernal RA, Stock D, Stewart AG Structure. 2016 Jan 28. pii: S0969-2126(16)00010-1. doi:, 10.1016/j.str.2015.12.016. PMID:26853941[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Chaston JJ, Smits C, Aragao D, Wong AS, Ahsan B, Sandin S, Molugu SK, Molugu SK, Bernal RA, Stock D, Stewart AG. Structural and Functional Insights into the Evolution and Stress Adaptation of Type II Chaperonins. Structure. 2016 Jan 28. pii: S0969-2126(16)00010-1. doi:, 10.1016/j.str.2015.12.016. PMID:26853941 doi:http://dx.doi.org/10.1016/j.str.2015.12.016
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