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4j5h

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==Crystal Structure of B. thuringiensis AiiA mutant F107W with N-decanoyl-L-homoserine bound at the active site==
==Crystal Structure of B. thuringiensis AiiA mutant F107W with N-decanoyl-L-homoserine bound at the active site==
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<StructureSection load='4j5h' size='340' side='right' caption='[[4j5h]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
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<StructureSection load='4j5h' size='340' side='right'caption='[[4j5h]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4j5h]] 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=4J5H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4J5H FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4j5h]] 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=4J5H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4J5H FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1K4:N-DECANOYL-L-HOMOSERINE'>1K4</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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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]] 1.45&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4j5f|4j5f]]</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=1K4:N-DECANOYL-L-HOMOSERINE'>1K4</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='gene'><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=1428 Bacillus thuringiensis])</td></tr>
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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=4j5h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j5h OCA], [https://pdbe.org/4j5h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4j5h RCSB], [https://www.ebi.ac.uk/pdbsum/4j5h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4j5h ProSAT]</span></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Quorum-quenching_N-acyl-homoserine_lactonase Quorum-quenching N-acyl-homoserine lactonase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.81 3.1.1.81] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4j5h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j5h OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4j5h RCSB], [http://www.ebi.ac.uk/pdbsum/4j5h PDBsum]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/AHLL_BACTU AHLL_BACTU] 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:15895999</ref>
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Autoinducer inactivator A (AiiA) is a metal-dependent N-acyl homoserine lactone hydrolase that displays broad substrate specificity but shows a preference for substrates with long N-acyl substitutions. Previously, crystal structures of AiiA in complex with the ring-opened product N-hexanoyl-l-homoserine revealed binding interactions near the metal center but did not identify a binding pocket for the N-acyl chains of longer substrates. Here we report the crystal structure of an AiiA mutant, F107W, determined in the presence and absence of N-decanoyl-l-homoserine. F107 is located in a hydrophobic cavity adjacent to the previously identified ligand binding pocket, and the F107W mutation results in the formation of an unexpected interaction with the ring-opened product. Notably, the structure reveals a previously unidentified hydrophobic binding pocket for the substrate's N-acyl chain. Two aromatic residues, F64 and F68, form a hydrophobic clamp, centered around the seventh carbon in the product-bound structure's decanoyl chain, making an interaction that would also be available for longer substrates, but not for shorter substrates. Steady-state kinetics using substrates of various lengths with AiiA bearing mutations at the hydrophobic clamp, including insertion of a redox-sensitive cysteine pair, confirms the importance of this hydrophobic feature for substrate preference. Identifying the specificity determinants of AiiA will aid the development of more selective quorum-quenching enzymes as tools and as potential therapeutics.
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A phenylalanine clamp controls substrate specificity in the quorum-quenching metallo-gamma-lactonase from Bacillus thuringiensis.,Liu CF, Liu D, Momb J, Thomas PW, Lajoie A, Petsko GA, Fast W, Ringe D Biochemistry. 2013 Mar 5;52(9):1603-10. doi: 10.1021/bi400050j. Epub 2013 Feb 20. PMID:23387521<ref>PMID:23387521</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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== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Bacillus thuringiensis]]
[[Category: Bacillus thuringiensis]]
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[[Category: Quorum-quenching N-acyl-homoserine lactonase]]
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[[Category: Large Structures]]
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[[Category: Fast, W]]
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[[Category: Fast W]]
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[[Category: Lajoie, A]]
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[[Category: Lajoie A]]
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[[Category: Liu, C F]]
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[[Category: Liu CF]]
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[[Category: Liu, D]]
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[[Category: Liu D]]
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[[Category: Momb, J]]
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[[Category: Momb J]]
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[[Category: Petsko, G A]]
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[[Category: Petsko GA]]
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[[Category: Ringe, D]]
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[[Category: Ringe D]]
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[[Category: Thomas, P W]]
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[[Category: Thomas PW]]
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[[Category: Aiia]]
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[[Category: Beta-hairpin loop]]
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[[Category: Dizinc hydrolase]]
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[[Category: Hydrolase-hydrolase substrate complex]]
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[[Category: Lactonase]]
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[[Category: N-acyl homoserine lactone]]
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[[Category: Quorum quenching]]
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[[Category: Substrate specificity]]
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Current revision

Crystal Structure of B. thuringiensis AiiA mutant F107W with N-decanoyl-L-homoserine bound at the active site

PDB ID 4j5h

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