Emily LythellReynier SuardíazPhilip HinchliffeChonnikan HanpaiboolSurawit VisitsatthawongA. Sofia F. OliveiraA. Sofia F. OliveiraEric J.M. LangPanida SurawatanawongVannajan Sanghiran LeeThanyada RungrotmongkolNatalie FeyJames SpencerAdrian J. MulhollandUniversity of MalayaChulalongkorn UniversityUniversidad Complutense de MadridUniversity of PortsmouthUniversity of BristolMahidol University2020-08-252020-08-252020-06-25Chemical Communications. Vol.56, No.50 (2020), 6874-68771364548X135973452-s2.0-85087096464https://repository.li.mahidol.ac.th/handle/123456789/57794© 2020 The Royal Society of Chemistry. 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.Mahidol UniversityChemical EngineeringChemistryMaterials ScienceArticleSCOPUS10.1039/d0cc02520h