4x5s
From Proteopedia
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| - | ''' | + | ==The crystal structure of an alpha carbonic anhydrase from the extremophilic bacterium Sulfurihydrogenibium azorense.== |
| + | <StructureSection load='4x5s' size='340' side='right' caption='[[4x5s]], [[Resolution|resolution]] 1.95Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4x5s]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4X5S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4X5S 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=PE8:3,6,9,12,15,18,21-HEPTAOXATRICOSANE-1,23-DIOL'>PE8</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=4x5s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x5s OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4x5s RCSB], [http://www.ebi.ac.uk/pdbsum/4x5s PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Two thermostable alpha-carbonic anhydrases (alpha-CAs) isolated from thermophilic Sulfurihydrogenibium spp., namely SspCA (from S. yellowstonensis) and SazCA (from S. azorense), were shown in a previous work to possess interesting complementary properties. SspCA was shown to have an exceptional thermal stability, whereas SazCA demonstrated to be the most active alpha-CA known to date for the CO2 hydration reaction. Here we report the crystallographic structure of SazCA and the identification of the structural features responsible for its high catalytic activity, by comparing it with SspCA structure. These data are of relevance for the design of engineered proteins showing higher stability and catalytic activity than other alpha-CAs known to date. | ||
| - | + | Crystal structure of the most catalytically effective carbonic anhydrase enzyme known, SazCA from the thermophilic bacterium Sulfurihydrogenibium azorense.,De Simone G, Monti SM, Alterio V, Buonanno M, De Luca V, Rossi M, Carginale V, Supuran CT, Capasso C, Di Fiore A Bioorg Med Chem Lett. 2015 May 1;25(9):2002-6. doi: 10.1016/j.bmcl.2015.02.068., Epub 2015 Mar 6. PMID:25817590<ref>PMID:25817590</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | [[Category: | + | </StructureSection> |
| + | [[Category: Carbonate dehydratase]] | ||
[[Category: Alterio, V]] | [[Category: Alterio, V]] | ||
| + | [[Category: Fiore, A Di]] | ||
| + | [[Category: Simone, G De]] | ||
| + | [[Category: Alpha bacterial carbonic anhydrase]] | ||
| + | [[Category: Enzyme-inhibitor complex]] | ||
| + | [[Category: Lyase]] | ||
Revision as of 12:09, 20 May 2015
The crystal structure of an alpha carbonic anhydrase from the extremophilic bacterium Sulfurihydrogenibium azorense.
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