The molecular structure and catalytic mechanism of a quorum-quenching N-acyl-L-homoserine lactone hydrolase

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dc.contributor.authorMyung Hee Kim-
dc.contributor.authorWon Chan Choi-
dc.contributor.authorHye Ok Kang-
dc.contributor.authorJong Suk Lee-
dc.contributor.authorB S Kang-
dc.contributor.authorK J Kim-
dc.contributor.authorZ S Derewenda-
dc.contributor.authorTae Kwang Oh-
dc.contributor.authorChoong Hwan Lee-
dc.contributor.authorJung-Kee Lee-
dc.date.accessioned2017-04-19T09:03:43Z-
dc.date.available2017-04-19T09:03:43Z-
dc.date.issued2005-
dc.identifier.issn0027-8424-
dc.identifier.uri10.1073/pnas.0504996102ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/7204-
dc.description.abstractIn 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-? resolution structure of the AHL-lactonase from Bacillus thuringiensis and a 1.7-? 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-β-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.-
dc.publisherNatl Acad Sciences-
dc.titleThe molecular structure and catalytic mechanism of a quorum-quenching N-acyl-L-homoserine lactone hydrolase-
dc.title.alternativeThe molecular structure and catalytic mechanism of a quorum-quenching N-acyl-L-homoserine lactone hydrolase-
dc.typeArticle-
dc.citation.titleProceedings of National Academy of Sciences of United States of America-
dc.citation.number49-
dc.citation.endPage17611-
dc.citation.startPage17606-
dc.citation.volume102-
dc.contributor.affiliatedAuthorMyung Hee Kim-
dc.contributor.affiliatedAuthorWon Chan Choi-
dc.contributor.affiliatedAuthorHye Ok Kang-
dc.contributor.affiliatedAuthorJong Suk Lee-
dc.contributor.affiliatedAuthorTae Kwang Oh-
dc.contributor.affiliatedAuthorChoong Hwan Lee-
dc.contributor.affiliatedAuthorJung-Kee Lee-
dc.contributor.alternativeName김명희-
dc.contributor.alternativeName최원찬-
dc.contributor.alternativeName강혜옥-
dc.contributor.alternativeName이종석-
dc.contributor.alternativeName강범식-
dc.contributor.alternativeName김경진-
dc.contributor.alternativeNameDerewenda-
dc.contributor.alternativeName오태광-
dc.contributor.alternativeName이충환-
dc.contributor.alternativeName이정기-
dc.identifier.bibliographicCitationProceedings of National Academy of Sciences of United States of America, vol. 102, no. 49, pp. 17606-17611-
dc.identifier.doi10.1073/pnas.0504996102-
dc.subject.keywordcrystal structure-
dc.subject.keywordlactonase-
dc.subject.keywordmetalloenzyme-
dc.subject.keywordquorum sensing-
dc.subject.localcrystal structure-
dc.subject.localCrystal structure-
dc.subject.locallactonase-
dc.subject.localMetalloenzyme-
dc.subject.localmetalloenzyme-
dc.subject.localquorum sensing-
dc.subject.localQuorum sensing-
dc.description.journalClassY-
Appears in Collections:
Division of Biomedical Research > Microbiome Convergence Research Center > 1. Journal Articles
Division of Biomedical Research > Metabolic Regulation Research Center > 1. Journal Articles
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