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| | <StructureSection load='3dha' size='340' side='right'caption='[[3dha]], [[Resolution|resolution]] 0.95Å' scene=''> | | <StructureSection load='3dha' size='340' side='right'caption='[[3dha]], [[Resolution|resolution]] 0.95Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3dha]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bactk Bactk]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DHA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DHA FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3dha]] 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=3DHA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DHA FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C6L:N-HEXANOYL-L-HOMOSERINE'>C6L</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 0.95Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2a7m|2a7m]], [[2r2d|2r2d]], [[3dhb|3dhb]], [[3dhc|3dhc]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C6L:N-HEXANOYL-L-HOMOSERINE'>C6L</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">aiiA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29339 BACTK])</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=3dha FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dha OCA], [https://pdbe.org/3dha PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3dha RCSB], [https://www.ebi.ac.uk/pdbsum/3dha PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3dha 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=3dha FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dha OCA], [https://pdbe.org/3dha PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3dha RCSB], [https://www.ebi.ac.uk/pdbsum/3dha PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3dha 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>
| + | [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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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bactk]] | + | [[Category: Bacillus thuringiensis serovar kurstaki]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Fast, W]] | + | [[Category: Fast W]] |
| - | [[Category: Liu, D]] | + | [[Category: Liu D]] |
| - | [[Category: Momb, J]] | + | [[Category: Momb J]] |
| - | [[Category: Moulin, A]] | + | [[Category: Moulin A]] |
| - | [[Category: Petsko, G A]] | + | [[Category: Petsko GA]] |
| - | [[Category: Ringe, D]] | + | [[Category: Ringe D]] |
| - | [[Category: Thomas, P W]] | + | [[Category: Thomas PW]] |
| - | [[Category: Ahl lactonase]]
| + | |
| - | [[Category: Alternative binding site]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: N-acyl homoserine lactone]]
| + | |
| - | [[Category: Product complex]]
| + | |
| - | [[Category: Quorum quenching]]
| + | |
| - | [[Category: Zinc bimetallohydrolase]]
| + | |
| Structural highlights
Function
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.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Enzymes capable of hydrolyzing N-acyl- l-homoserine lactones (AHLs) used in some bacterial quorum-sensing pathways are of considerable interest for their ability to block undesirable phenotypes. Most known AHL hydrolases that catalyze ring opening (AHL lactonases) are members of the metallo-beta-lactamase enzyme superfamily and rely on a dinuclear zinc site for catalysis and stability. Here we report the three-dimensional structures of three product complexes formed with the AHL lactonase from Bacillus thuringiensis. Structures of the lactonase bound with two different concentrations of the ring-opened product of N-hexanoyl- l-homoserine lactone are determined at 0.95 and 1.4 A resolution and exhibit different product configurations. A structure of the ring-opened product of the non-natural N-hexanoyl- l-homocysteine thiolactone at 1.3 A resolution is also determined. On the basis of these product-bound structures, a substrate-binding model is presented that differs from previous proposals. Additionally, the proximity of the product to active-site residues and observed changes in protein conformation and metal coordination provide insight into the catalytic mechanism of this quorum-quenching metalloenzyme.
Mechanism of the quorum-quenching lactonase (AiiA) from Bacillus thuringiensis. 1. Product-bound structures.,Liu D, Momb J, Thomas PW, Moulin A, Petsko GA, Fast W, Ringe D Biochemistry. 2008 Jul 22;47(29):7706-14. PMID:18627129[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kim MH, Choi WC, Kang HO, Lee JS, Kang BS, Kim KJ, Derewenda ZS, Oh TK, Lee CH, Lee JK. The molecular structure and catalytic mechanism of a quorum-quenching N-acyl-L-homoserine lactone hydrolase. Proc Natl Acad Sci U S A. 2005 Dec 6;102(49):17606-11. Epub 2005 Nov 28. PMID:16314577
- ↑ Liu D, Momb J, Thomas PW, Moulin A, Petsko GA, Fast W, Ringe D. Mechanism of the quorum-quenching lactonase (AiiA) from Bacillus thuringiensis. 1. Product-bound structures. Biochemistry. 2008 Jul 22;47(29):7706-14. PMID:18627129 doi:10.1021/bi800368y
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