DC Field | Value | Language |
---|---|---|
dc.contributor.author | Kim, JY | - |
dc.contributor.author | Jung, HI | - |
dc.contributor.author | An, YJ | - |
dc.contributor.author | Hun, JH | - |
dc.contributor.author | Suh, PG | - |
dc.contributor.author | Lee, HS | - |
dc.contributor.author | Lee, SH | - |
dc.contributor.author | Cha, SS | - |
dc.date.accessioned | 2016-04-01T01:56:34Z | - |
dc.date.available | 2016-04-01T01:56:34Z | - |
dc.date.created | 2009-02-28 | - |
dc.date.issued | 2006-05 | - |
dc.identifier.issn | 0950-382X | - |
dc.identifier.other | 2006-OAK-0000005897 | - |
dc.identifier.uri | https://oasis.postech.ac.kr/handle/2014.oak/24054 | - |
dc.description.abstract | The emergence and dissemination of extended-spectrum (ES) beta-lactamases induce therapeutic failure and a lack of eradication of clinical isolates even by third-generation beta-lactam antibiotics like ceftazidime. CMY-10 is a plasmid-encoded class C beta-lactamase with a wide spectrum of substrates. Unlike the well-studied class C ES beta-lactamase from Enterobacter cloacae GC1, the Omega-loop does not affect the active site conformation and the catalytic activity of CMY-10. Instead, a three-amino-acid deletion in the R2-loop appears to be responsible for the ES activity of CMY-10. According to the crystal structure solved at 1.55 angstrom resolution, the deletion significantly widens the R2 active site, which accommodates the R2 side-chains of beta-lactam antibiotics. This observation led us to demonstrate the hydrolysing activity of CMY-10 towards imipenem with a long R2 substituent. The forced mutational analyses of P99 beta-lactamase reveal that the introduction of deletion mutations into the R2-loop is able to extend the substrate spectrum of class C non-ES beta-lactamases, which is compatible with the isolation of natural class C ES enzymes harbouring deletion mutations in the R2-loop. Consequently, the opening of the R2 active site by the deletion of some residues in the R2-loop can be considered as an operative molecular strategy of class C beta-lactamases to extend their substrate spectrum. | - |
dc.description.statementofresponsibility | X | - |
dc.language | English | - |
dc.publisher | BLACKWELL PUBLISHING | - |
dc.relation.isPartOf | MOLECULAR MICROBIOLOGY | - |
dc.subject | TRANSITION-STATE ANALOG | - |
dc.subject | ENTEROBACTER-CLOACAE P99 | - |
dc.subject | CLINICAL ISOLATE | - |
dc.subject | CRYSTAL-STRUCTURE | - |
dc.subject | OMEGA-LOOP | - |
dc.subject | INHIBITOR DESIGN | - |
dc.subject | SPECIFICITY | - |
dc.subject | RESISTANCE | - |
dc.subject | ACID | - |
dc.subject | MUTAGENESIS | - |
dc.title | Structural basis for the extended substrate spectrum of CMY-10, a plasmid-encoded class C beta-lactamase | - |
dc.type | Article | - |
dc.contributor.college | 생명과학과 | - |
dc.identifier.doi | 10.1111/J.1365-2958. | - |
dc.author.google | Kim, JY | - |
dc.author.google | Jung, HI | - |
dc.author.google | An, YJ | - |
dc.author.google | Hun, JH | - |
dc.author.google | Suh, PG | - |
dc.author.google | Lee, HS | - |
dc.author.google | Lee, SH | - |
dc.author.google | Cha, SS | - |
dc.relation.issue | 4 | - |
dc.relation.startpage | 907 | - |
dc.relation.lastpage | 916 | - |
dc.contributor.id | 10052640 | - |
dc.relation.journal | MOLECULAR MICROBIOLOGY | - |
dc.relation.index | SCI급, SCOPUS 등재논문 | - |
dc.relation.sci | SCI | - |
dc.collections.name | Journal Papers | - |
dc.type.rims | ART | - |
dc.identifier.bibliographicCitation | MOLECULAR MICROBIOLOGY, v.60, no.4, pp.907 - 916 | - |
dc.identifier.wosid | 000237297800009 | - |
dc.date.tcdate | 2019-01-01 | - |
dc.citation.endPage | 916 | - |
dc.citation.number | 4 | - |
dc.citation.startPage | 907 | - |
dc.citation.title | MOLECULAR MICROBIOLOGY | - |
dc.citation.volume | 60 | - |
dc.contributor.affiliatedAuthor | Suh, PG | - |
dc.description.journalClass | 1 | - |
dc.description.journalClass | 1 | - |
dc.description.wostc | 73 | - |
dc.type.docType | Article | - |
dc.subject.keywordPlus | TRANSITION-STATE ANALOG | - |
dc.subject.keywordPlus | ENTEROBACTER-CLOACAE P99 | - |
dc.subject.keywordPlus | CLINICAL ISOLATE | - |
dc.subject.keywordPlus | CRYSTAL-STRUCTURE | - |
dc.subject.keywordPlus | OMEGA-LOOP | - |
dc.subject.keywordPlus | INHIBITOR DESIGN | - |
dc.subject.keywordPlus | SPECIFICITY | - |
dc.subject.keywordPlus | RESISTANCE | - |
dc.subject.keywordPlus | ACID | - |
dc.subject.keywordPlus | MUTAGENESIS | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Microbiology | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalResearchArea | Microbiology | - |
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