Resistance to the "last resort" antibiotic colistin: a single-zinc mechanism for phosphointermediate formation in MCR enzymes.
Resistance to the "last resort" antibiotic colistin: a single-zinc mechanism for phosphointermediate formation in MCR enzymes.
复制标题
DOI：
10.1039/d0cc02520h
复制
发表时间：
2020-05
影响因子：
4.9
通讯作者：
Emily Lythell;R. Suardíaz;P. Hinchliffe;Chonnikan Hanpaibool;Surawit Visitsatthawong;Sofia Oliveira;Eric J. M. Lang;Panida Surawatanawong;V. Lee;T. Rungrotmongkol;Natalie Fey;J. Spencer;A. Mulholland
中科院分区：
文献类型：
--
作者：
Emily Lythell;R. Suardíaz;P. Hinchliffe;Chonnikan Hanpaibool;Surawit Visitsatthawong;Sofia Oliveira;Eric J. M. Lang;Panida Surawatanawong;V. Lee;T. Rungrotmongkol;Natalie Fey;J. Spencer;A. Mulholland
MCR（移动的粘菌素抗性）酶催化磷酸乙醇胺（PEA）添加到细菌脂质A，威胁到“最后手段”抗生素粘菌素。分子动力学和密度泛函理论模拟表明，单锌MCR支持PEA转移到Thr285受体，定位MCR作为一个单核，而不是多核成员的碱性磷酸酶超家族。
MCR (mobile colistin resistance) enzymes catalyse phosphoethanolamine (PEA) addition to bacterial lipid A, threatening the "last-resort" antibiotic colistin. Molecular dynamics and density functional theory simulations indicate that monozinc MCR supports PEA transfer to the Thr285 acceptor, positioning MCR as a mono- rather than multinuclear member of the alkaline phosphatase superfamily.