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

DOI: 10.1107/S2053230X17009669 DOI Help

Authors: Katie Coates (University of Bristol) , Timothy R. Walsh (Cardiff Institute of Infection and Immunity) , James Spencer (University of Bristol) , Philip Hinchliffe (University of Bristol)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acta Crystallographica Section F Structural Biology Communications , VOL 73 , PAGES 443 - 449

State: Published (Approved)
Published: August 2017
Diamond Proposal Number(s): 12342

Open Access Open Access

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 Keywords: MCR-1; antibiotic resistance; colistin; MCR-2; polymixin

Subject Areas: Biology and Bio-materials, Medicine


Instruments: I04-Macromolecular Crystallography

Documents:
no5117.pdf