2a7m
From Proteopedia
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<StructureSection load='2a7m' size='340' side='right'caption='[[2a7m]], [[Resolution|resolution]] 1.60Å' scene=''> | <StructureSection load='2a7m' size='340' side='right'caption='[[2a7m]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2a7m]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[2a7m]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_thuringiensis_serovar_kurstaki Bacillus thuringiensis serovar kurstaki]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A7M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2A7M FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=2a7m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a7m OCA], [https://pdbe.org/2a7m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2a7m RCSB], [https://www.ebi.ac.uk/pdbsum/2a7m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2a7m ProSAT]</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=2a7m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a7m OCA], [https://pdbe.org/2a7m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2a7m RCSB], [https://www.ebi.ac.uk/pdbsum/2a7m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2a7m ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/AHLLA_BACTK AHLLA_BACTK] Catalyzes hydrolysis of N-hexanoyl-(S)-homoserine lactone, but not the R-enantiomer. Hydrolyzes short- and long-chain N-acyl homoserine lactones with or without 3-oxo substitution at C3, has maximum activity on C10-AHL.<ref>PMID:16314577</ref> | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2a7m ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2a7m ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The three-dimensional structure of the N-acyl-l-homoserine lactone hydrolase (AHL lactonase) from Bacillus thuringiensis has been determined, by using single-wavelength anomalous dispersion (SAD) phasing, to 1.6-angstroms resolution. AHLs are produced by many Gram-negative bacteria as signaling molecules used in quorum-sensing pathways that indirectly sense cell density and regulate communal behavior. Because of their importance in pathogenicity, quorum-sensing pathways have been suggested as potential targets for the development of novel therapeutics. Quorum-sensing can be disrupted by enzymes evolved to degrade these lactones, such as AHL lactonases. These enzymes are members of the metallo-beta-lactamase superfamily and contain two zinc ions in their active sites. The zinc ions are coordinated to a number of ligands, including a single oxygen of a bridging carboxylate and a bridging water/hydroxide ion, thought to be the nucleophile that hydrolyzes the AHLs to ring-opened products, which can no longer act as quorum signals. | ||
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| - | Three-dimensional structure of the quorum-quenching N-acyl homoserine lactone hydrolase from Bacillus thuringiensis.,Liu D, Lepore BW, Petsko GA, Thomas PW, Stone EM, Fast W, Ringe D Proc Natl Acad Sci U S A. 2005 Aug 16;102(33):11882-7. Epub 2005 Aug 8. PMID:16087890<ref>PMID:16087890</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 2a7m" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Bacillus thuringiensis serovar kurstaki]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Fast | + | [[Category: Fast W]] |
| - | [[Category: Lepore | + | [[Category: Lepore BW]] |
| - | [[Category: Liu | + | [[Category: Liu D]] |
| - | [[Category: Petsko | + | [[Category: Petsko GA]] |
| - | [[Category: Ringe | + | [[Category: Ringe D]] |
| - | [[Category: Stone | + | [[Category: Stone EM]] |
| - | [[Category: Thomas | + | [[Category: Thomas PW]] |
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Current revision
1.6 Angstrom Resolution Structure of the Quorum-Quenching N-Acyl Homoserine Lactone Hydrolase of Bacillus thuringiensis
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