| http://purl.uniprot.org/citations/16314577 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16314577 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16314577 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/16314577 | http://www.w3.org/2000/01/rdf-schema#comment | "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."xsd:string |
| http://purl.uniprot.org/citations/16314577 | http://purl.org/dc/terms/identifier | "doi:10.1073/pnas.0504996102"xsd:string |
| http://purl.uniprot.org/citations/16314577 | http://purl.org/dc/terms/identifier | "doi:10.1073/pnas.0504996102"xsd:string |
| http://purl.uniprot.org/citations/16314577 | http://purl.uniprot.org/core/author | "Lee J.S."xsd:string |
| http://purl.uniprot.org/citations/16314577 | http://purl.uniprot.org/core/author | "Lee J.S."xsd:string |
| http://purl.uniprot.org/citations/16314577 | http://purl.uniprot.org/core/author | "Oh T.K."xsd:string |
| http://purl.uniprot.org/citations/16314577 | http://purl.uniprot.org/core/author | "Oh T.K."xsd:string |
| http://purl.uniprot.org/citations/16314577 | http://purl.uniprot.org/core/author | "Derewenda Z.S."xsd:string |
| http://purl.uniprot.org/citations/16314577 | http://purl.uniprot.org/core/author | "Derewenda Z.S."xsd:string |
| http://purl.uniprot.org/citations/16314577 | http://purl.uniprot.org/core/author | "Lee J.K."xsd:string |
| http://purl.uniprot.org/citations/16314577 | http://purl.uniprot.org/core/author | "Lee J.K."xsd:string |
| http://purl.uniprot.org/citations/16314577 | http://purl.uniprot.org/core/author | "Kim K.J."xsd:string |
| http://purl.uniprot.org/citations/16314577 | http://purl.uniprot.org/core/author | "Kim K.J."xsd:string |
| http://purl.uniprot.org/citations/16314577 | http://purl.uniprot.org/core/author | "Lee C.H."xsd:string |
| http://purl.uniprot.org/citations/16314577 | http://purl.uniprot.org/core/author | "Lee C.H."xsd:string |
| http://purl.uniprot.org/citations/16314577 | http://purl.uniprot.org/core/author | "Choi W.C."xsd:string |
| http://purl.uniprot.org/citations/16314577 | http://purl.uniprot.org/core/author | "Choi W.C."xsd:string |
| http://purl.uniprot.org/citations/16314577 | http://purl.uniprot.org/core/author | "Kang B.S."xsd:string |
| http://purl.uniprot.org/citations/16314577 | http://purl.uniprot.org/core/author | "Kang B.S."xsd:string |
| http://purl.uniprot.org/citations/16314577 | http://purl.uniprot.org/core/author | "Kang H.O."xsd:string |
| http://purl.uniprot.org/citations/16314577 | http://purl.uniprot.org/core/author | "Kang H.O."xsd:string |
| http://purl.uniprot.org/citations/16314577 | http://purl.uniprot.org/core/author | "Kim M.H."xsd:string |