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Resistance to the “last resort” antibiotic colistin: a single-zinc mechanism for phosphointermediate formation in MCR enzymes

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dc.contributor.authorLythell, Emily
dc.contributor.authorSuardíaz Delrío, Reynier
dc.contributor.authorHinchliffe, Philip
dc.contributor.authorHanpaibool, Chonnikan
dc.contributor.authorVisitsatthawong, Surawit
dc.contributor.authorOliveira, Sofia
dc.contributor.authorLang, Eric
dc.contributor.authorSurawatanawong, Panida
dc.contributor.authorLee, Vannajan Sanghiran
dc.contributor.authorRungrotmongkol, Thanyada
dc.contributor.authorFey, Natalie
dc.contributor.authorSpencer, James
dc.contributor.authorMulholland, Adrian
dc.date.accessioned2024-01-11T07:50:40Z
dc.date.available2024-01-11T07:50:40Z
dc.date.issued2020
dc.description.abstractMCR (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.
dc.description.departmentDepto. de Química Física
dc.description.facultyFac. de Ciencias Químicas
dc.description.refereedTRUE
dc.description.sponsorshipMahidol University (Thailand)
dc.description.sponsorshipUniversity of Bristol
dc.description.sponsorshipThailand Research Fund
dc.description.sponsorshipMedical Research Council
dc.description.sponsorshipUniversiti Malaya (Malaysia)
dc.description.sponsorshipResearch England
dc.description.sponsorshipRoyal Society of Chemistry
dc.description.statuspub
dc.identifier.citationLythell, Emily, et al. «Resistance to the “Last Resort” Antibiotic Colistin: A Single-Zinc Mechanism for Phosphointermediate Formation in MCR Enzymes». Chemical Communications, vol. 56, n.o 50, 2020, pp. 6874-77. https://doi.org/10.1039/D0CC02520H.
dc.identifier.doi10.1039/d0cc02520h
dc.identifier.essn1364-548X
dc.identifier.issn1359-7345
dc.identifier.officialurlhttps://doi.org/10.1039/d0cc02520h
dc.identifier.urihttps://hdl.handle.net/20.500.14352/92414
dc.issue.number50
dc.journal.titleChemical Communications
dc.language.isoeng
dc.page.final6877
dc.page.initial6874
dc.publisherRoyal Society of Chemistry
dc.relation.projectIDEP/M013219/1
dc.relation.projectIDEP/M022609/1
dc.relation.projectIDEP/M027546/1
dc.relation.projectIDRSA6280041
dc.relation.projectIDBB/J014400/1
dc.relation.projectIDBB/L01386X/1
dc.relation.projectIDBB/M012107/1
dc.relation.projectIDMR/P007295/1
dc.relation.projectIDGPF062B-2018
dc.relation.projectIDR19-3409
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 Internationalen
dc.rights.accessRightsrestricted access
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/
dc.subject.cdu546
dc.subject.keywordAlkaline Phosphatase
dc.subject.keywordAnti-Bacterial Agents
dc.subject.keywordBacterial Proteins
dc.subject.keywordColistin
dc.subject.keywordDrug Resistance
dc.subject.keywordBacterial
dc.subject.keywordEthanolamines
dc.subject.keywordLipid A
dc.subject.keywordMolecular Dynamics Simulation
dc.subject.keywordZinc
dc.subject.ucmQuímica
dc.subject.unesco23 Química
dc.titleResistance to the “last resort” antibiotic colistin: a single-zinc mechanism for phosphointermediate formation in MCR enzymes
dc.typejournal article
dc.type.hasVersionVoR
dc.volume.number56
dspace.entity.typePublication
relation.isAuthorOfPublication8b0c8e63-584d-4205-a5aa-81107b9bd474
relation.isAuthorOfPublication.latestForDiscovery8b0c8e63-584d-4205-a5aa-81107b9bd474

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