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6yjn
From Proteopedia
(Difference between revisions)
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==Crystal structure of beta carbonic anhydrase from the pathogenic bacterium Burkholderia pseudomallei.== | ==Crystal structure of beta carbonic anhydrase from the pathogenic bacterium Burkholderia pseudomallei.== | ||
| - | <StructureSection load='6yjn' size='340' side='right'caption='[[6yjn]]' scene=''> | + | <StructureSection load='6yjn' size='340' side='right'caption='[[6yjn]], [[Resolution|resolution]] 2.70Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6YJN OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6YJN FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6yjn]] 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=6YJN OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6YJN FirstGlance]. <br> |
| - | </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=6yjn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6yjn OCA], [http://pdbe.org/6yjn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6yjn RCSB], [http://www.ebi.ac.uk/pdbsum/6yjn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6yjn ProSAT]</span></td></tr> | + | </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='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='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://proteopedia.org/fgij/fg.htm?mol=6yjn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6yjn OCA], [http://pdbe.org/6yjn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6yjn RCSB], [http://www.ebi.ac.uk/pdbsum/6yjn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6yjn ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:32408533</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6yjn" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Carbonic anhydrase 3D structures|Carbonic anhydrase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Bacillus pseudomallei whitmore 1913]] | ||
| + | [[Category: Carbonate dehydratase]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Angeli A]] | + | [[Category: Angeli, A]] |
| - | [[Category: Ferraroni M]] | + | [[Category: Ferraroni, M]] |
| + | [[Category: Beta carbonic anhydrase]] | ||
| + | [[Category: Burkholderia pseudomallei]] | ||
| + | [[Category: Lyase]] | ||
Revision as of 08:13, 11 November 2020
Crystal structure of beta carbonic anhydrase from the pathogenic bacterium Burkholderia pseudomallei.
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