2a7m
From Proteopedia
(Difference between revisions)
m (Protected "2a7m" [edit=sysop:move=sysop]) |
|||
Line 1: | Line 1: | ||
- | [[ | + | ==1.6 Angstrom Resolution Structure of the Quorum-Quenching N-Acyl Homoserine Lactone Hydrolase of Bacillus thuringiensis== |
+ | <StructureSection load='2a7m' size='340' side='right' caption='[[2a7m]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[2a7m]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2A7M FirstGlance]. <br> | ||
+ | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br> | ||
+ | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">aiia ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29339 Bacillus thuringiensis serovar kurstaki])</td></tr> | ||
+ | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2a7m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a7m OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2a7m RCSB], [http://www.ebi.ac.uk/pdbsum/2a7m PDBsum]</span></td></tr> | ||
+ | <table> | ||
+ | == Evolutionary Conservation == | ||
+ | [[Image:Consurf_key_small.gif|200px|right]] | ||
+ | Check<jmol> | ||
+ | <jmolCheckbox> | ||
+ | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a7/2a7m_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
+ | <text>to colour the structure by Evolutionary Conservation</text> | ||
+ | </jmolCheckbox> | ||
+ | </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/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
+ | <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. | ||
- | + | 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> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
- | + | </StructureSection> | |
- | + | ||
- | == | + | |
- | < | + | |
[[Category: Bacillus thuringiensis serovar kurstaki]] | [[Category: Bacillus thuringiensis serovar kurstaki]] | ||
[[Category: Fast, W.]] | [[Category: Fast, W.]] |
Revision as of 00:36, 30 September 2014
1.6 Angstrom Resolution Structure of the Quorum-Quenching N-Acyl Homoserine Lactone Hydrolase of Bacillus thuringiensis
|