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| ==Crystal Structure of Citrate Synthase from Pyrobaculum aerophilum== | | ==Crystal Structure of Citrate Synthase from Pyrobaculum aerophilum== |
- | <StructureSection load='2ibp' size='340' side='right' caption='[[2ibp]], [[Resolution|resolution]] 1.60Å' scene=''> | + | <StructureSection load='2ibp' size='340' side='right'caption='[[2ibp]], [[Resolution|resolution]] 1.60Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[2ibp]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrae Pyrae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IBP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2IBP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2ibp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrobaculum_aerophilum_str._IM2 Pyrobaculum aerophilum str. IM2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IBP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IBP FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 1.6Å</td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PAE1689 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=178306 PYRAE])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ibp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ibp OCA], [https://pdbe.org/2ibp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ibp RCSB], [https://www.ebi.ac.uk/pdbsum/2ibp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ibp ProSAT]</span></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=2ibp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ibp OCA], [http://pdbe.org/2ibp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ibp RCSB], [http://www.ebi.ac.uk/pdbsum/2ibp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ibp ProSAT]</span></td></tr> | + | |
| </table> | | </table> |
| + | == Function == |
| + | [https://www.uniprot.org/uniprot/Q8ZWP2_PYRAE Q8ZWP2_PYRAE] |
| == Evolutionary Conservation == | | == Evolutionary Conservation == |
| [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| ==See Also== | | ==See Also== |
- | *[[Citrate Synthase|Citrate Synthase]] | + | *[[Citrate Synthase 3D structures|Citrate Synthase 3D structures]] |
| == References == | | == References == |
| <references/> | | <references/> |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Pyrae]] | + | [[Category: Large Structures]] |
- | [[Category: Boutz, D R]] | + | [[Category: Pyrobaculum aerophilum str. IM2]] |
- | [[Category: Cascio, D]] | + | [[Category: Boutz DR]] |
- | [[Category: Yeates, T O]] | + | [[Category: Cascio D]] |
- | [[Category: Catenane]] | + | [[Category: Yeates TO]] |
- | [[Category: Citrate synthase]]
| + | |
- | [[Category: Disulfide bond]]
| + | |
- | [[Category: Homodimer]]
| + | |
- | [[Category: Thermophilic]]
| + | |
- | [[Category: Transferase]]
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| Structural highlights
Function
Q8ZWP2_PYRAE
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
A growing number of organisms have been discovered inhabiting extreme environments, including temperatures in excess of 100 degrees C. How cellular proteins from such organisms retain their native folds under extreme conditions is still not fully understood. Recent computational and structural studies have identified disulfide bonding as an important mechanism for stabilizing intracellular proteins in certain thermophilic microbes. Here, we present the first proteomic analysis of intracellular disulfide bonding in the hyperthermophilic archaeon Pyrobaculum aerophilum. Our study reveals that the utilization of disulfide bonds extends beyond individual proteins to include many protein-protein complexes. We report the 1.6 A crystal structure of one such complex, a citrate synthase homodimer. The structure contains two intramolecular disulfide bonds, one per subunit, which result in the cyclization of each protein chain in such a way that the two chains are topologically interlinked, rendering them inseparable. This unusual feature emphasizes the variety and sophistication of the molecular mechanisms that can be achieved by evolution.
Discovery of a thermophilic protein complex stabilized by topologically interlinked chains.,Boutz DR, Cascio D, Whitelegge J, Perry LJ, Yeates TO J Mol Biol. 2007 May 18;368(5):1332-44. Epub 2007 Mar 6. PMID:17395198[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Boutz DR, Cascio D, Whitelegge J, Perry LJ, Yeates TO. Discovery of a thermophilic protein complex stabilized by topologically interlinked chains. J Mol Biol. 2007 May 18;368(5):1332-44. Epub 2007 Mar 6. PMID:17395198 doi:10.1016/j.jmb.2007.02.078
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