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

Coates, Katie, Walsh, Timothy R. ORCID: https://orcid.org/0000-0003-4315-4096, Spencer, James and Hinchliffe, Philip 2017. 1.12 A˚ resolution crystal structure of the catalytic domain of the plasmid-mediated colistin resistance determinant MCR-2. Acta Crystallographica Section F Structural Biology Communications 73 (8) , pp. 443-449. 10.1107/S2053230X17009669

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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.

Item Type:	Article
Status:	Published
Schools:	Medicine
Publisher:	International Union of Crystallography
ISSN:	2053-230X
Date of First Compliant Deposit:	14 August 2017
Date of Acceptance:	30 June 2017
Last Modified:	02 May 2023 23:42
URI:	https://orca.cardiff.ac.uk/id/eprint/103558

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