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| | <StructureSection load='6yl7' size='340' side='right'caption='[[6yl7]], [[Resolution|resolution]] 3.17Å' scene=''> | | <StructureSection load='6yl7' size='340' side='right'caption='[[6yl7]], [[Resolution|resolution]] 3.17Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6yl7]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_pseudomallei"_whitmore_1913 "bacillus pseudomallei" whitmore 1913]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6YL7 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6YL7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6yl7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Burkholderia_pseudomallei Burkholderia pseudomallei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6YL7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6YL7 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 3.17Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">can_1, can_2, BOC42_16450, CXQ84_19645, DF122_01465, ERS013345_01543, SAMEA1968934_03740 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=28450 "Bacillus pseudomallei" Whitmore 1913])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[https://proteopedia.org/fgij/fg.htm?mol=6yl7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6yl7 OCA], [https://pdbe.org/6yl7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6yl7 RCSB], [https://www.ebi.ac.uk/pdbsum/6yl7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6yl7 ProSAT]</span></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=6yl7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6yl7 OCA], [http://pdbe.org/6yl7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6yl7 RCSB], [http://www.ebi.ac.uk/pdbsum/6yl7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6yl7 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A069AXA0_BURPE A0A069AXA0_BURPE] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus pseudomallei whitmore 1913]] | |
| - | [[Category: Carbonate dehydratase]] | |
| - | [[Category: Large Structures]] | |
| - | [[Category: Angeli, A]] | |
| - | [[Category: Ferraroni, M]] | |
| - | [[Category: Beta carbonic anhydrase]] | |
| | [[Category: Burkholderia pseudomallei]] | | [[Category: Burkholderia pseudomallei]] |
| - | [[Category: Carbonic anhydrase]] | + | [[Category: Large Structures]] |
| - | [[Category: Lyase]] | + | [[Category: Angeli A]] |
| | + | [[Category: Ferraroni M]] |
| Structural highlights
Function
A0A069AXA0_BURPE
Publication Abstract from PubMed
Carbonic anhydrase (CA) is a zinc enzyme that catalyzes the reversible conversion of carbon dioxide to bicarbonate and proton. Currently, CA inhibitors are widely used as antiglaucoma, anticancer, and anti-obesity drugs and for the treatment of neurological disorders. Recently, the potential use of CA inhibitors to fight infections caused by protozoa, fungi, and bacteria has emerged as a new research line. In this article, the X-ray crystal structure of beta-CA from Burkholderia pseudomallei was reported. The X-ray crystal structure of this new enzyme was solved at 2.7 A resolution, revealing a tetrameric type II beta-CA with a "closed" active site in which the zinc is tetrahedrally coordinated to Cys46, Asp48, His102, and Cys105. B. pseudomallei is known to encode at least two CAs, a beta-CA, and a gamma-CA. These proteins, playing a pivotal role in its life cycle and pathogenicity, offer a novel therapeutic opportunity to obtain antibiotics with a different mechanism of action. Furthermore, the new structure can provide a clear view of the beta-CA mechanism of action and the possibility to find selective inhibitors for this class of CAs.
Crystal Structure of a Tetrameric Type II beta-Carbonic Anhydrase from the Pathogenic Bacterium Burkholderia pseudomallei.,Angeli A, Ferraroni M, Pinteala M, Maier SS, Simionescu BC, Carta F, Del Prete S, Capasso C, Supuran CT Molecules. 2020 May 12;25(10). pii: molecules25102269. doi:, 10.3390/molecules25102269. PMID:32408533[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Angeli A, Ferraroni M, Pinteala M, Maier SS, Simionescu BC, Carta F, Del Prete S, Capasso C, Supuran CT. Crystal Structure of a Tetrameric Type II beta-Carbonic Anhydrase from the Pathogenic Bacterium Burkholderia pseudomallei. Molecules. 2020 May 12;25(10). pii: molecules25102269. doi:, 10.3390/molecules25102269. PMID:32408533 doi:http://dx.doi.org/10.3390/molecules25102269
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