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1.12 Å resolution crystal structure of the catalytic domain of the plasmid-mediated colistin resistance determinant MCR-2

MCR-2 confers resistance to colistin, a ‘last-line’ antibiotic against extensively resistant Gram-negative pathogens. It is a plasmid-encoded phosphoethanol­amine transferase that is closely related to MCR-1. To understand the diversity in the MCR family, the 1.12 Å resolution crystal structure of t...

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Detalles Bibliográficos
Autores principales: Coates, Katie, Walsh, Timothy R., Spencer, James, Hinchliffe, Philip
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5544000/
https://www.ncbi.nlm.nih.gov/pubmed/28777086
http://dx.doi.org/10.1107/S2053230X17009669
Descripción
Sumario:MCR-2 confers resistance to colistin, a ‘last-line’ antibiotic against extensively resistant Gram-negative pathogens. It is a plasmid-encoded phosphoethanol­amine transferase that is closely related to MCR-1. To understand the diversity in the MCR family, the 1.12 Å resolution crystal structure of the catalytic domain of MCR-2 was determined. Variable amino acids are located distant from both the di-zinc active site and the membrane-proximal face. The exceptionally high resolution will provide an accurate starting model for further mechanistic studies.