2a7m: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
New page: left|200px<br /><applet load="2a7m" size="350" color="white" frame="true" align="right" spinBox="true" caption="2a7m, resolution 1.60Å" /> '''1.6 Angstrom Resolut...
 
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
 
(13 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:2a7m.gif|left|200px]]<br /><applet load="2a7m" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2a7m, resolution 1.60&Aring;" />
'''1.6 Angstrom Resolution Structure of the Quorum-Quenching N-Acyl Homoserine Lactone Hydrolase of Bacillus thuringiensis'''<br />


==Overview==
==1.6 Angstrom Resolution Structure of the Quorum-Quenching N-Acyl Homoserine Lactone Hydrolase of Bacillus thuringiensis==
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.
<StructureSection load='2a7m' size='340' side='right'caption='[[2a7m]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<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>
2A7M is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_thuringiensis_serovar_kurstaki Bacillus thuringiensis serovar kurstaki] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A7M OCA].  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
 
<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>
==Reference==
<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>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16087890 16087890]
</table>
== 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 ==
[[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/main_output.php?pdb_ID=2a7m ConSurf].
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacillus thuringiensis serovar kurstaki]]
[[Category: Bacillus thuringiensis serovar kurstaki]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Fast, W.]]
[[Category: Fast W]]
[[Category: Lepore, B.W.]]
[[Category: Lepore BW]]
[[Category: Liu, D.]]
[[Category: Liu D]]
[[Category: Petsko, G.A.]]
[[Category: Petsko GA]]
[[Category: Ringe, D.]]
[[Category: Ringe D]]
[[Category: Stone, E.M.]]
[[Category: Stone EM]]
[[Category: Thomas, P.W.]]
[[Category: Thomas PW]]
[[Category: GOL]]
[[Category: ZN]]
[[Category: bimetallo di-zinc]]
[[Category: bimetallohydrolase]]
[[Category: hydrolase]]
[[Category: lactonase acyl homoserine]]
[[Category: n-acyl]]
[[Category: quorum quenching n-acyl]]
[[Category: zinc]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 17:56:13 2008''
Retrieved from "https://proteopedia.org/2a7m"