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

Philip Hinchliffe; James Spencer

doi:10.1107/S2053230X17009669

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

Philip Hinchliffe, James Spencer

Research output: Contribution to journal › Article (Academic Journal) › peer-review

18 Citations (Scopus)

324 Downloads (Pure)

Abstract

MCR-2 confers resistance to colistin, a ‘last-line’ antibiotic against extensively-resistant Gram-negative pathogens. It is a plasmid-encoded phosphoethanolamine transferase closely related to MCR 1. To understand the diversity in the MCR-family we have determined the 1.12 Å resolution crystal structure of the MCR-2 catalytic domain. Variable amino acids are located distant from both the di-zinc active site and membrane-proximal face. The exceptionally high resolution will provide an accurate starting model for further mechanistic studies.

Original language	English
Journal	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
DOIs	https://doi.org/10.1107/S2053230X17009669
Publication status	Published - 26 Jul 2017

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10.1107/S2053230X17009669

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title = "1.12 {\AA} resolution crystal structure of the catalytic domain of the plasmid-mediated colistin resistance determinant MCR-2",

abstract = "MCR-2 confers resistance to colistin, a {\textquoteleft}last-line{\textquoteright} antibiotic against extensively-resistant Gram-negative pathogens. It is a plasmid-encoded phosphoethanolamine transferase closely related to MCR 1. To understand the diversity in the MCR-family we have determined the 1.12 {\AA} resolution crystal structure of the MCR-2 catalytic domain. Variable amino acids are located distant from both the di-zinc active site and membrane-proximal face. The exceptionally high resolution will provide an accurate starting model for further mechanistic studies.",

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year = "2017",

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doi = "10.1107/S2053230X17009669",

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T1 - 1.12 Å resolution crystal structure of the catalytic domain of the plasmid-mediated colistin resistance determinant MCR-2

AU - Hinchliffe, Philip

AU - Spencer, James

PY - 2017/7/26

Y1 - 2017/7/26

N2 - MCR-2 confers resistance to colistin, a ‘last-line’ antibiotic against extensively-resistant Gram-negative pathogens. It is a plasmid-encoded phosphoethanolamine transferase closely related to MCR 1. To understand the diversity in the MCR-family we have determined the 1.12 Å resolution crystal structure of the MCR-2 catalytic domain. Variable amino acids are located distant from both the di-zinc active site and membrane-proximal face. The exceptionally high resolution will provide an accurate starting model for further mechanistic studies.

AB - MCR-2 confers resistance to colistin, a ‘last-line’ antibiotic against extensively-resistant Gram-negative pathogens. It is a plasmid-encoded phosphoethanolamine transferase closely related to MCR 1. To understand the diversity in the MCR-family we have determined the 1.12 Å resolution crystal structure of the MCR-2 catalytic domain. Variable amino acids are located distant from both the di-zinc active site and membrane-proximal face. The exceptionally high resolution will provide an accurate starting model for further mechanistic studies.

U2 - 10.1107/S2053230X17009669

DO - 10.1107/S2053230X17009669

M3 - Article (Academic Journal)

C2 - 28777086

JO - Acta Crystallographica Section F: Structural Biology and Crystallization Communications

JF - Acta Crystallographica Section F: Structural Biology and Crystallization Communications

SN - 1744-3091

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