2btn

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[[Image:2btn.png|left|200px]]
 
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==Crystal Structure and Catalytic Mechanism of the Quorum-Quenching N- Acyl Homoserine Lactone Hydrolase==
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The line below this paragraph, containing "STRUCTURE_2btn", creates the "Structure Box" on the page.
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<StructureSection load='2btn' size='340' side='right'caption='[[2btn]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2btn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_thuringiensis Bacillus thuringiensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BTN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BTN FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
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<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>
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{{STRUCTURE_2btn| PDB=2btn | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2btn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2btn OCA], [https://pdbe.org/2btn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2btn RCSB], [https://www.ebi.ac.uk/pdbsum/2btn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2btn ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bt/2btn_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=2btn ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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In many Gram-negative bacteria, including a number of pathogens such as Pseudomonas aeruginosa and Erwinia carotovora, virulence factor production and biofilm formation are linked to the quorum-sensing systems that use diffusible N-acyl-L-homoserine lactones (AHLs) as intercellular messenger molecules. A number of organisms also contain genes coding for lactonases that hydrolyze AHLs into inactive products, thereby blocking the quorum-sensing systems. Consequently, these enzymes attract intense interest for the development of antiinfection therapies. However, the catalytic mechanism of AHL-lactonase is poorly understood and subject to controversy. We here report a 2.0-angstroms resolution structure of the AHL-lactonase from Bacillus thuringiensis and a 1.7-angstroms crystal structure of its complex with L-homoserine lactone. Despite limited sequence similarity, the enzyme shows remarkable structural similarities to glyoxalase II and RNase Z proteins, members of the metallo-beta-lactamase superfamily. We present experimental evidence that AHL-lactonase is a metalloenzyme containing two zinc ions involved in catalysis, and we propose a catalytic mechanism for bacterial metallo-AHL-lactonases.
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===CRYSTAL STRUCTURE AND CATALYTIC MECHANISM OF THE QUORUM-QUENCHING N-ACYL HOMOSERINE LACTONE HYDROLASE===
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The molecular structure and catalytic mechanism of a quorum-quenching N-acyl-L-homoserine lactone hydrolase.,Kim MH, Choi WC, Kang HO, Lee JS, Kang BS, Kim KJ, Derewenda ZS, Oh TK, Lee CH, Lee JK Proc Natl Acad Sci U S A. 2005 Dec 6;102(49):17606-11. Epub 2005 Nov 28. PMID:16314577<ref>PMID:16314577</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_16314577}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2btn" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 16314577 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_16314577}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[2btn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_thuringiensis Bacillus thuringiensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BTN OCA].
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==Reference==
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<ref group="xtra">PMID:16314577</ref><ref group="xtra">PMID:15894524</ref><references group="xtra"/>
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[[Category: Bacillus thuringiensis]]
[[Category: Bacillus thuringiensis]]
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[[Category: Choi, W C.]]
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[[Category: Large Structures]]
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[[Category: Derewenda, Z S.]]
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[[Category: Choi WC]]
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[[Category: Kang, B S.]]
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[[Category: Derewenda ZS]]
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[[Category: Kang, H O.]]
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[[Category: Kang BS]]
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[[Category: Kim, K J.]]
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[[Category: Kang HO]]
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[[Category: Kim, M H.]]
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[[Category: Kim KJ]]
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[[Category: Lee, C H.]]
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[[Category: Kim MH]]
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[[Category: Lee, J K.]]
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[[Category: Lee CH]]
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[[Category: Lee, J S.]]
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[[Category: Lee JK]]
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[[Category: Oh, T K.]]
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[[Category: Lee JS]]
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[[Category: Hydrolase]]
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[[Category: Oh TK]]
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[[Category: N-acyl homoserine lactone hydrolase]]
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[[Category: Quorum sensing]]
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Current revision

Crystal Structure and Catalytic Mechanism of the Quorum-Quenching N- Acyl Homoserine Lactone Hydrolase

PDB ID 2btn

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