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1.12 Å resolution crystal structure of the catalytic domain of the plasmid‐mediated colistin resistance determinant MCR‐2
Author(s) -
Coates Katie,
Walsh Timothy R.,
Spencer James,
Hinchliffe Philip
Publication year - 2017
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x17009669
Subject(s) - colistin , plasmid , mcr 1 , transferase , resolution (logic) , biology , crystal structure , microbiology and biotechnology , chemistry , genetics , antibiotics , escherichia coli , crystallography , gene , biochemistry , enzyme , enterobacteriaceae , computer science , artificial intelligence
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.