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

1.12 Å resolution crystal structure of the catalytic domain of the plasmid‐mediated colistin... 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Acta Crystallographica Section F Wiley

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

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Publisher
Wiley
Copyright
Copyright © 2017 Wiley Subscription Services
ISSN
2053-230X
eISSN
2053-230X
DOI
10.1107/S2053230X17009669
pmid
28777086
Publisher site
See Article on Publisher Site

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.

Journal

Acta Crystallographica Section FWiley

Published: Jan 1, 2017

Keywords: ; ; ; ;

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