| http://purl.uniprot.org/citations/23387521 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/23387521 | http://www.w3.org/2000/01/rdf-schema#comment | "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."xsd:string |
| http://purl.uniprot.org/citations/23387521 | http://purl.org/dc/terms/identifier | "doi:10.1021/bi400050j"xsd:string |
| http://purl.uniprot.org/citations/23387521 | http://purl.uniprot.org/core/author | "Liu D."xsd:string |
| http://purl.uniprot.org/citations/23387521 | http://purl.uniprot.org/core/author | "Liu C.F."xsd:string |
| http://purl.uniprot.org/citations/23387521 | http://purl.uniprot.org/core/author | "Petsko G.A."xsd:string |
| http://purl.uniprot.org/citations/23387521 | http://purl.uniprot.org/core/author | "Ringe D."xsd:string |
| http://purl.uniprot.org/citations/23387521 | http://purl.uniprot.org/core/author | "Fast W."xsd:string |
| http://purl.uniprot.org/citations/23387521 | http://purl.uniprot.org/core/author | "Momb J."xsd:string |
| http://purl.uniprot.org/citations/23387521 | http://purl.uniprot.org/core/author | "Thomas P.W."xsd:string |
| http://purl.uniprot.org/citations/23387521 | http://purl.uniprot.org/core/author | "Lajoie A."xsd:string |
| http://purl.uniprot.org/citations/23387521 | http://purl.uniprot.org/core/date | "2013"xsd:gYear |
| http://purl.uniprot.org/citations/23387521 | http://purl.uniprot.org/core/name | "Biochemistry"xsd:string |
| http://purl.uniprot.org/citations/23387521 | http://purl.uniprot.org/core/pages | "1603-1610"xsd:string |
| http://purl.uniprot.org/citations/23387521 | http://purl.uniprot.org/core/title | "A phenylalanine clamp controls substrate specificity in the quorum-quenching metallo-gamma-lactonase from Bacillus thuringiensis."xsd:string |
| http://purl.uniprot.org/citations/23387521 | http://purl.uniprot.org/core/volume | "52"xsd:string |
| http://purl.uniprot.org/citations/23387521 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/23387521 |
| http://purl.uniprot.org/citations/23387521 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/23387521 |
| http://purl.uniprot.org/uniprot/#_A3FJ64-mappedCitation-23387521 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/23387521 |
| http://purl.uniprot.org/uniprot/A3FJ64 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/23387521 |