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Structural and biochemical analyses of an aminoglycoside 2′-N-acetyltransferase from Mycolicibacterium smegmatis

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dc.contributor.authorJeong, Chang Sook-
dc.contributor.authorHwang, Jisub-
dc.contributor.authorDo, Hackwon-
dc.contributor.authorCha, Sun-Shin-
dc.contributor.authorOh, Tae-Jin-
dc.contributor.authorKim, Hak Jun-
dc.contributor.authorPark, Hyun Ho-
dc.contributor.authorLee, Jun Hyuck-
dc.date.accessioned2021-05-03T08:46:05Z-
dc.date.available2021-05-03T08:46:05Z-
dc.date.issued2020-12-
dc.identifier.urihttps://repository.kopri.re.kr/handle/201206/11810-
dc.description.abstractThe expression of aminoglycoside-modifying enzymes represents a survival strategy of antibiotic-resistant bacteria. Aminoglycoside 2'-N-acetyltransferase (AAC(2')) neutralizes aminoglycoside drugs by acetylation of their 2' amino groups in an acetyl coenzyme A (CoA)-dependent manner. To understand the structural features and molecular mechanism underlying AAC(2') activity, we overexpressed, purified, and crystallized AAC(2') from Mycolicibacterium smegmatis (AAC(2')-Id) and determined the crystal structures of its apo-form and ternary complexes with CoA and four different aminoglycosides (gentamicin, sisomicin, neomycin, and paromomycin). These AAC(2')-Id structures unraveled the binding modes of different aminoglycosides, explaining the broad substrate specificity of the enzyme. Comparative structural analysis showed that the α4-helix and β8?β9 loop region undergo major conformational changes upon CoA and substrate binding. Additionally, structural comparison between the present paromomycin-bound AAC(2')-Id structure and the previously reported paromomycin-bound AAC(6')-Ib and 30S ribosome structures revealed the structural features of paromomycin that are responsible for its antibiotic activity and AAC binding. Taken together, these results provide useful information for designing AAC(2') inhibitors and for the chemical modification of aminoglycosides.en_US
dc.languageEnglishen_US
dc.language.isoen_USen_US
dc.subjectScience & Technologyen_US
dc.subject.classification해당사항없음en_US
dc.titleStructural and biochemical analyses of an aminoglycoside 2′-N-acetyltransferase from Mycolicibacterium smegmatisen_US
dc.title.alternative항생물질 변형 및 항생제 내성에 관여하는 aminoglycoside 2'-N-acetyltransferase 효소의 삼차구조와 생화학적 특성 연구en_US
dc.typeArticleen_US
dc.identifier.bibliographicCitationJeong, Chang Sook, et al. 2020. "Structural and biochemical analyses of an aminoglycoside 2′-N-acetyltransferase from Mycolicibacterium smegmatis". <em>SCIENTIFIC REPORTS</em>, 10(1): 1-14.en_US
dc.citation.titleSCIENTIFIC REPORTSen_US
dc.citation.volume10en_US
dc.citation.number1en_US
dc.identifier.doi10.1038/s41598-020-78699-z-
dc.citation.startPage1en_US
dc.citation.endPage14en_US
dc.description.articleClassificationSCI-
dc.description.jcrRateJCR 2018:21.739en_US
dc.subject.keywordX-ray crystallographyen_US
dc.subject.keywordaminoglycoside acetyltransferaseen_US
dc.subject.keywordantibioticsen_US
dc.subject.keywordcrystal structureen_US
dc.identifier.localId2020-0207-
dc.identifier.scopusid2-s2.0-85097382573-
dc.identifier.wosid000608953600012-
Appears in Collections  
2020-2020, Development of potential candidates as antibiotics based on polar genetic resources (20-20) / Lee, Jun Hyuck (PM20030)
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