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| | ==The crystal structure of an alpha Carbonic Anhydrase from the extremophilic bacterium Sulfurihydrogenibium yellowstonense YO3AOP1== | | ==The crystal structure of an alpha Carbonic Anhydrase from the extremophilic bacterium Sulfurihydrogenibium yellowstonense YO3AOP1== |
| - | <StructureSection load='4g7a' size='340' side='right' caption='[[4g7a]], [[Resolution|resolution]] 1.80Å' scene=''> | + | <StructureSection load='4g7a' size='340' side='right'caption='[[4g7a]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4g7a]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Sulsy Sulsy]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G7A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4G7A FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4g7a]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sulfurihydrogenibium_sp._YO3AOP1 Sulfurihydrogenibium sp. YO3AOP1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G7A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4G7A FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AZM:5-ACETAMIDO-1,3,4-THIADIAZOLE-2-SULFONAMIDE'>AZM</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AZM:5-ACETAMIDO-1,3,4-THIADIAZOLE-2-SULFONAMIDE'>AZM</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1kop|1kop]], [[1ca2|1ca2]]</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=4g7a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g7a OCA], [https://pdbe.org/4g7a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4g7a RCSB], [https://www.ebi.ac.uk/pdbsum/4g7a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4g7a ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SYO3AOP1_0578 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=436114 SULSY])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Carbonate_dehydratase Carbonate dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.1 4.2.1.1] </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=4g7a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g7a OCA], [http://pdbe.org/4g7a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4g7a RCSB], [http://www.ebi.ac.uk/pdbsum/4g7a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4g7a ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/B2V8E3_SULSY B2V8E3_SULSY] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Carbonic anhydrase|Carbonic anhydrase]] | + | *[[Carbonic anhydrase 3D structures|Carbonic anhydrase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Carbonate dehydratase]] | + | [[Category: Large Structures]] |
| - | [[Category: Sulsy]] | + | [[Category: Sulfurihydrogenibium sp. YO3AOP1]] |
| - | [[Category: Fiore, A Di]]
| + | [[Category: De Simone G]] |
| - | [[Category: Simone, G De]] | + | [[Category: Di Fiore A]] |
| - | [[Category: Lyase]] | + | |
| Structural highlights
Function
B2V8E3_SULSY
Publication Abstract from PubMed
SspCA, a novel `extremo-alpha-carbonic anhydrase' isolated from the thermophilic bacterium Sulfurihydrogenibium yellowstonense YO3AOP1, is an efficient catalyst for the hydration of CO2 and presents exceptional thermostability. Indeed, SspCA retains a high catalytic activity even after being heated to 343-373 K for several hours. Here, the crystallographic structure of this alpha-carbonic anhydrase (alpha-CA) is reported and the factors responsible for its function at high temperature are elucidated. In particular, the study suggests that increased structural compactness, together with an increased number of charged residues on the protein surface and a greater number of ionic networks, seem to be the key factors involved in the higher thermostability of this enzyme with respect to its mesophilic homologues. These findings are of extreme importance, since they provide a structural basis for the understanding of the mechanisms responsible for thermal stability in the alpha-CA family for the first time. The data obtained offer a tool that can be exploited to engineer alpha-CAs in order to obtain enzymes with enhanced thermostability for use in the harsh conditions of the CO2 capture and sequestration processes.
X-ray structure of the first `extremo-alpha-carbonic anhydrase', a dimeric enzyme from the thermophilic bacterium Sulfurihydrogenibium yellowstonense YO3AOP1.,Di Fiore A, Capasso C, De Luca V, Monti SM, Carginale V, Supuran CT, Scozzafava A, Pedone C, Rossi M, De Simone G Acta Crystallogr D Biol Crystallogr. 2013 Jun;69(Pt 6):1150-9. doi:, 10.1107/S0907444913007208. Epub 2013 May 16. PMID:23695259[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Di Fiore A, Capasso C, De Luca V, Monti SM, Carginale V, Supuran CT, Scozzafava A, Pedone C, Rossi M, De Simone G. X-ray structure of the first `extremo-alpha-carbonic anhydrase', a dimeric enzyme from the thermophilic bacterium Sulfurihydrogenibium yellowstonense YO3AOP1. Acta Crystallogr D Biol Crystallogr. 2013 Jun;69(Pt 6):1150-9. doi:, 10.1107/S0907444913007208. Epub 2013 May 16. PMID:23695259 doi:10.1107/S0907444913007208
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