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Wide-open conformation of UDP-MurNc-tripeptide ligase revealed by the substrate-free structure of MurE from Acinetobacter baumannii

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dc.contributor.authorJung, Kyoung Ho-
dc.contributor.authorKim, Yeon-Gil-
dc.contributor.authorKim, Chang Min-
dc.contributor.authorHa, Hyun Ji-
dc.contributor.authorLee, Chang Sup-
dc.contributor.authorLee, Jun Hyuck-
dc.contributor.authorPark, Hyun Ho-
dc.date.accessioned2021-05-04T05:41:37Z-
dc.date.available2021-05-04T05:41:37Z-
dc.date.issued2021-01-
dc.identifier.urihttps://repository.kopri.re.kr/handle/201206/11815-
dc.description.abstractMurE ligase catalyzes the attachment of meso-diaminopimelic acid to the UDP-MurNAc-L -Ala-D -Glu using ATP and producing UDP-MurNAc-L -Ala-D -Glu-meso-A2 pm during bacterial cell wall biosynthesis. Owing to the critical role of this enzyme, MurE is considered an attractive target for antibacterial drugs. Despite extensive studies on MurE ligase, the structural dynamics of its conformational changes are still elusive. In this study, we present the substrate-free structure of MurE from Acinetobacter baumannii, which is an antibiotic-resistant superbacterium that has threatened global public health. The structure revealed that MurE has a wide-open conformation and undergoes wide-open, intermediately closed, and fully closed dynamic conformational transition. Unveiling structural dynamics of MurE will help to understand the working mechanism of this ligase and to design next-generation antibiotics targeting MurE.en_US
dc.languageEnglishen_US
dc.language.isoen_USen_US
dc.subjectBiochemistry & Molecular Biologyen_US
dc.subjectBiophysicsen_US
dc.subjectCell Biologyen_US
dc.subject.classification해당사항없음en_US
dc.titleWide-open conformation of UDP-MurNc-tripeptide ligase revealed by the substrate-free structure of MurE from Acinetobacter baumanniien_US
dc.title.alternative병원균 (Acinetobacter baumannii) 유래 항생물질 타겟 단백질인 MurE 효소의 기질이 결합되어 있지않은 열려진 형태의 구조 규명en_US
dc.typeArticleen_US
dc.identifier.bibliographicCitationJung, Kyoung Ho, et al. 2021. "Wide-open conformation of UDP-MurNc-tripeptide ligase revealed by the substrate-free structure of MurE from Acinetobacter baumannii". <em>FEBS LETTERS</em>, 595(2): 275-283.en_US
dc.citation.titleFEBS LETTERSen_US
dc.citation.volume595en_US
dc.citation.number2en_US
dc.identifier.doi10.1002/1873-3468.14007-
dc.citation.startPage275en_US
dc.citation.endPage283en_US
dc.description.articleClassificationSCIE-
dc.description.jcrRateJCR 2019:33.803en_US
dc.subject.keywordAcinetobacter baumanniien_US
dc.subject.keywordATP-dependent ligaseen_US
dc.subject.keywordcell wall peptidoglycan biosynthesisen_US
dc.subject.keywordcrystal structureen_US
dc.subject.keywordMurEen_US
dc.identifier.localId2020-0200-
dc.identifier.scopusid2-s2.0-85097028413-
dc.identifier.wosid000595231700001-
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2020-2020, Development of potential candidates as antibiotics based on polar genetic resources (20-20) / Lee, Jun Hyuck (PM20030)
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