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


ABSTRACT: 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.

SUBMITTER: Coates K 

PROVIDER: S-EPMC5544000 | biostudies-literature | 2017 Aug

REPOSITORIES: biostudies-literature

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

Coates Katie K   Walsh Timothy R TR   Spencer James J   Hinchliffe Philip P  

Acta crystallographica. Section F, Structural biology communications 20170726 Pt 8


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  ...[more]

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