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| | <StructureSection load='1o7x' size='340' side='right'caption='[[1o7x]], [[Resolution|resolution]] 2.70Å' scene=''> | | <StructureSection load='1o7x' size='340' side='right'caption='[[1o7x]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1o7x]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/'saccharolobus_solfataricus' 'saccharolobus solfataricus']. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O7X OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1O7X FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1o7x]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus Saccharolobus solfataricus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O7X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1O7X FirstGlance]. <br> |
| - | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Citrate_(Si)-synthase Citrate (Si)-synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.3.1 2.3.3.1] </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]] 2.7Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1o7x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o7x OCA], [http://pdbe.org/1o7x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1o7x RCSB], [http://www.ebi.ac.uk/pdbsum/1o7x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1o7x 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=1o7x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o7x OCA], [https://pdbe.org/1o7x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1o7x RCSB], [https://www.ebi.ac.uk/pdbsum/1o7x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1o7x ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/CISY_SACS2 CISY_SACS2] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Saccharolobus solfataricus]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bell, G S]] | + | [[Category: Saccharolobus solfataricus]] |
| - | [[Category: Connaris, H]] | + | [[Category: Bell GS]] |
| - | [[Category: Danson, M J]] | + | [[Category: Connaris H]] |
| - | [[Category: Hough, D W]] | + | [[Category: Danson MJ]] |
| - | [[Category: Russell, R J.M]] | + | [[Category: Hough DW]] |
| - | [[Category: Taylor, G L]] | + | [[Category: Russell RJM]] |
| - | [[Category: Lyase]]
| + | [[Category: Taylor GL]] |
| - | [[Category: Synthase]]
| + | |
| - | [[Category: Tricarboxylic acid cycle]]
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| Structural highlights
Function
CISY_SACS2
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 citrate synthase from the thermophilic Archaeon Sulfolobus solfataricus (optimum growth temperature = 85 degrees C) has been determined, extending the number of crystal structures of citrate synthase from different organisms to a total of five that span the temperature range over which life exists (from psychrophile to hyperthermophile). Detailed structural analysis has revealed possible molecular mechanisms that determine the different stabilities of the five proteins. The key to these mechanisms is the precise structural location of the additional interactions. As one ascends the temperature ladder, the subunit interface of this dimeric enzyme and loop regions are reinforced by complex electrostatic interactions, and there is a reduced exposure of hydrophobic surface. These observations reveal a progressive pattern of stabilization through multiple additional interactions at solvent exposed, loop and interfacial regions.
Stepwise adaptations of citrate synthase to survival at life's extremes. From psychrophile to hyperthermophile.,Bell GS, Russell RJ, Connaris H, Hough DW, Danson MJ, Taylor GL Eur J Biochem. 2002 Dec;269(24):6250-60. PMID:12473121[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Bell GS, Russell RJ, Connaris H, Hough DW, Danson MJ, Taylor GL. Stepwise adaptations of citrate synthase to survival at life's extremes. From psychrophile to hyperthermophile. Eur J Biochem. 2002 Dec;269(24):6250-60. PMID:12473121
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