6sut | pdb_00006sut
From Proteopedia
Crystal structure of phosphothreonine MCR-2
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Structural highlights
FunctionPublication Abstract from PubMedMCR (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. Resistance to the "last resort" antibiotic colistin: a single-zinc mechanism for phosphointermediate formation in MCR enzymes.,Lythell E, Suardiaz R, Hinchliffe P, Hanpaibool C, Visitsatthawong S, Oliveira ASF, Lang EJM, Surawatanawong P, Lee VS, Rungrotmongkol T, Fey N, Spencer J, Mulholland AJ Chem Commun (Camb). 2020 Jun 23;56(50):6874-6877. doi: 10.1039/d0cc02520h. PMID:32432618[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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