6ksl
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Staphylococcus aureus lipase - S116A inactive mutant== | |
| + | <StructureSection load='6ksl' size='340' side='right'caption='[[6ksl]], [[Resolution|resolution]] 2.59Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6ksl]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KSL OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6KSL FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BUA:BUTANOIC+ACID'>BUA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=DAO:LAURIC+ACID'>DAO</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/Triacylglycerol_lipase Triacylglycerol lipase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3] </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=6ksl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ksl OCA], [http://pdbe.org/6ksl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ksl RCSB], [http://www.ebi.ac.uk/pdbsum/6ksl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ksl ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Staphylococcus aureus lipase (SAL), a triacylglycerol esterase, is an important virulence factor and may be a therapeutic target for infectious diseases. Herein, we determined the 3D structure of native SAL, the mutated S116A inactive form, and the inhibitor complex using the anti-obesity drug orlistat to aid in drug development. The determined crystal structures showed a typical alpha/beta hydrolase motif with a dimeric form. Fatty acids bound near the active site in native SAL and inactive S116A mutant structures. We found that orlistat potently inhibits SAL activity, and it covalently bound to the catalytic Ser116 residue. This is the first report detailing orlistat-lipase binding. It provides structure-based information on the production of potent anti-SAL drugs and lipase inhibitors. These results also indicated that orlistat can be repositioned to treat bacterial diseases. | ||
| - | + | Crystal structure of pathogenic Staphylococcus aureus lipase complex with the anti-obesity drug orlistat.,Kitadokoro K, Tanaka M, Hikima T, Okuno Y, Yamamoto M, Kamitani S Sci Rep. 2020 Mar 25;10(1):5469. doi: 10.1038/s41598-020-62427-8. PMID:32214208<ref>PMID:32214208</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6ksl" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Triacylglycerol lipase]] | ||
| + | [[Category: Kamitani, S]] | ||
| + | [[Category: Kitadokoro, K]] | ||
| + | [[Category: Tanaka, M]] | ||
| + | [[Category: Fatty acid binding]] | ||
| + | [[Category: Hydrolase]] | ||
Revision as of 06:48, 8 April 2020
Staphylococcus aureus lipase - S116A inactive mutant
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