DC Field | Value | Language |
---|---|---|
dc.contributor.author | Myung Hee Kim | - |
dc.contributor.author | Won Chan Choi | - |
dc.contributor.author | Hye Ok Kang | - |
dc.contributor.author | Jong Suk Lee | - |
dc.contributor.author | B S Kang | - |
dc.contributor.author | K J Kim | - |
dc.contributor.author | Z S Derewenda | - |
dc.contributor.author | Tae Kwang Oh | - |
dc.contributor.author | Choong Hwan Lee | - |
dc.contributor.author | Jung-Kee Lee | - |
dc.date.accessioned | 2017-04-19T09:03:43Z | - |
dc.date.available | 2017-04-19T09:03:43Z | - |
dc.date.issued | 2005 | - |
dc.identifier.issn | 0027-8424 | - |
dc.identifier.uri | 10.1073/pnas.0504996102 | ko |
dc.identifier.uri | https://oak.kribb.re.kr/handle/201005/7204 | - |
dc.description.abstract | 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-? 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.publisher | Natl Acad Sciences | - |
dc.title | The molecular structure and catalytic mechanism of a quorum-quenching N-acyl-L-homoserine lactone hydrolase | - |
dc.title.alternative | The molecular structure and catalytic mechanism of a quorum-quenching N-acyl-L-homoserine lactone hydrolase | - |
dc.type | Article | - |
dc.citation.title | Proceedings of National Academy of Sciences of United States of America | - |
dc.citation.number | 49 | - |
dc.citation.endPage | 17611 | - |
dc.citation.startPage | 17606 | - |
dc.citation.volume | 102 | - |
dc.contributor.affiliatedAuthor | Myung Hee Kim | - |
dc.contributor.affiliatedAuthor | Won Chan Choi | - |
dc.contributor.affiliatedAuthor | Hye Ok Kang | - |
dc.contributor.affiliatedAuthor | Jong Suk Lee | - |
dc.contributor.affiliatedAuthor | Tae Kwang Oh | - |
dc.contributor.affiliatedAuthor | Choong Hwan Lee | - |
dc.contributor.affiliatedAuthor | Jung-Kee Lee | - |
dc.contributor.alternativeName | 김명희 | - |
dc.contributor.alternativeName | 최원찬 | - |
dc.contributor.alternativeName | 강혜옥 | - |
dc.contributor.alternativeName | 이종석 | - |
dc.contributor.alternativeName | 강범식 | - |
dc.contributor.alternativeName | 김경진 | - |
dc.contributor.alternativeName | Derewenda | - |
dc.contributor.alternativeName | 오태광 | - |
dc.contributor.alternativeName | 이충환 | - |
dc.contributor.alternativeName | 이정기 | - |
dc.identifier.bibliographicCitation | Proceedings of National Academy of Sciences of United States of America, vol. 102, no. 49, pp. 17606-17611 | - |
dc.identifier.doi | 10.1073/pnas.0504996102 | - |
dc.subject.keyword | crystal structure | - |
dc.subject.keyword | lactonase | - |
dc.subject.keyword | metalloenzyme | - |
dc.subject.keyword | quorum sensing | - |
dc.subject.local | crystal structure | - |
dc.subject.local | Crystal structure | - |
dc.subject.local | lactonase | - |
dc.subject.local | Metalloenzyme | - |
dc.subject.local | metalloenzyme | - |
dc.subject.local | quorum sensing | - |
dc.subject.local | Quorum sensing | - |
dc.description.journalClass | Y | - |
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