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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Autores principales: Coates, Katie, Walsh, Timothy R., Spencer, James, Hinchliffe, Philip
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2017
Materias:
Research Communications
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
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author Coates, Katie
Walsh, Timothy R.
Spencer, James
Hinchliffe, Philip
author_facet Coates, Katie
Walsh, Timothy R.
Spencer, James
Hinchliffe, Philip
author_sort Coates, Katie
collection PubMed
description 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.
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spelling pubmed-55440002017-08-25 1.12 Å resolution crystal structure of the catalytic domain of the plasmid-mediated colistin resistance determinant MCR-2 Coates, Katie Walsh, Timothy R. Spencer, James Hinchliffe, Philip Acta Crystallogr F Struct Biol Commun Research Communications 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. International Union of Crystallography 2017-07-26 /pmc/articles/PMC5544000/ /pubmed/28777086 http://dx.doi.org/10.1107/S2053230X17009669 Text en © Coates et al. 2017 http://creativecommons.org/licenses/by/2.0/uk/ This is an open-access article distributed under the terms of the Creative Commons Attribution (CC-BY) Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.http://creativecommons.org/licenses/by/2.0/uk/
spellingShingle Research Communications
Coates, Katie
Walsh, Timothy R.
Spencer, James
Hinchliffe, Philip
1.12 Å resolution crystal structure of the catalytic domain of the plasmid-mediated colistin resistance determinant MCR-2
title 1.12 Å resolution crystal structure of the catalytic domain of the plasmid-mediated colistin resistance determinant MCR-2
title_full 1.12 Å resolution crystal structure of the catalytic domain of the plasmid-mediated colistin resistance determinant MCR-2
title_fullStr 1.12 Å resolution crystal structure of the catalytic domain of the plasmid-mediated colistin resistance determinant MCR-2
title_full_unstemmed 1.12 Å resolution crystal structure of the catalytic domain of the plasmid-mediated colistin resistance determinant MCR-2
title_short 1.12 Å resolution crystal structure of the catalytic domain of the plasmid-mediated colistin resistance determinant MCR-2
title_sort 1.12 å resolution crystal structure of the catalytic domain of the plasmid-mediated colistin resistance determinant mcr-2
topic Research Communications
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5544000/
https://www.ncbi.nlm.nih.gov/pubmed/28777086
http://dx.doi.org/10.1107/S2053230X17009669
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