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Resistance to the "last resort" antibiotic colistin: a single-zinc mechanism for phosphointermediate formation in MCR enzymes.
Lythell, Emily; Suardíaz, Reynier; Hinchliffe, Philip; Hanpaibool, Chonnikan; Visitsatthawong, Surawit; Oliveira, A Sofia F; Lang, Eric J M; Surawatanawong, Panida; Lee, Vannajan Sanghiran; Rungrotmongkol, Thanyada; Fey, Natalie; Spencer, James; Mulholland, Adrian J.
Afiliación
  • Lythell E; Centre for Computational Chemistry, School of Chemistry, University of Bristol, Cantock's Close, Bristol, BS8 1TS, UK. Adrian.Mulholland@bristol.ac.uk and School of Cellular and Molecular Medicine, University of Bristol, University Walk, Bristol, BS8 1TD, UK. Jim.Spencer@bristol.ac.uk.
  • Suardíaz R; Centre for Computational Chemistry, School of Chemistry, University of Bristol, Cantock's Close, Bristol, BS8 1TS, UK. Adrian.Mulholland@bristol.ac.uk and School of Biochemistry, University of Bristol, University Walk, Bristol, BS8 1TD, UK and Centre for Enzyme Innovation, School of Biological Scien
  • Hinchliffe P; School of Cellular and Molecular Medicine, University of Bristol, University Walk, Bristol, BS8 1TD, UK. Jim.Spencer@bristol.ac.uk.
  • Hanpaibool C; Structural and Computational Biology Research Unit, Department of Biochemistry, Faculty of Science, Chulalongkorn University, Bangkok 10330, Thailand.
  • Visitsatthawong S; Department of Chemistry and Center of Excellence for Innovation in Chemistry, Faculty of Science, Mahidol University, Bangkok 10400, Thailand.
  • Oliveira ASF; Centre for Computational Chemistry, School of Chemistry, University of Bristol, Cantock's Close, Bristol, BS8 1TS, UK. Adrian.Mulholland@bristol.ac.uk and School of Biochemistry, University of Bristol, University Walk, Bristol, BS8 1TD, UK.
  • Lang EJM; Centre for Computational Chemistry, School of Chemistry, University of Bristol, Cantock's Close, Bristol, BS8 1TS, UK. Adrian.Mulholland@bristol.ac.uk.
  • Surawatanawong P; Department of Chemistry and Center of Excellence for Innovation in Chemistry, Faculty of Science, Mahidol University, Bangkok 10400, Thailand.
  • Lee VS; Department of Chemistry, Faculty of Science, University of Malaya, Kuala Lumpur 50603, Malaysia.
  • Rungrotmongkol T; Structural and Computational Biology Research Unit, Department of Biochemistry, Faculty of Science, Chulalongkorn University, Bangkok 10330, Thailand and Program in Bioinformatics and Computational Biology, Graduate School, Chulalongkorn University, Bangkok 10330, Thailand.
  • Fey N; Centre for Computational Chemistry, School of Chemistry, University of Bristol, Cantock's Close, Bristol, BS8 1TS, UK. Adrian.Mulholland@bristol.ac.uk.
  • Spencer J; School of Cellular and Molecular Medicine, University of Bristol, University Walk, Bristol, BS8 1TD, UK. Jim.Spencer@bristol.ac.uk.
  • Mulholland AJ; Centre for Computational Chemistry, School of Chemistry, University of Bristol, Cantock's Close, Bristol, BS8 1TS, UK. Adrian.Mulholland@bristol.ac.uk.
Chem Commun (Camb) ; 56(50): 6874-6877, 2020 Jun 23.
Article en En | MEDLINE | ID: mdl-32432618
ABSTRACT
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.
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Texto completo: 1 Base de datos: MEDLINE Asunto principal: Proteínas Bacterianas / Zinc / Colistina / Farmacorresistencia Bacteriana / Fosfatasa Alcalina / Antibacterianos Idioma: En Revista: Chem Commun (Camb) Asunto de la revista: QUIMICA Año: 2020 Tipo del documento: Article País de afiliación: Reino Unido
Texto completo
Imprimir
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Texto completo: 1 Base de datos: MEDLINE Asunto principal: Proteínas Bacterianas / Zinc / Colistina / Farmacorresistencia Bacteriana / Fosfatasa Alcalina / Antibacterianos Idioma: En Revista: Chem Commun (Camb) Asunto de la revista: QUIMICA Año: 2020 Tipo del documento: Article País de afiliación: Reino Unido