5MX9

High resolution crystal structure of the MCR-2 catalytic domain

Summary for 5MX9

• Entry DOI: 10.2210/pdb5mx9/pdb
• Descriptor: Phosphatidylethanolamine transferase Mcr-2, ZINC ION, GLYCEROL, ... (4 entities in total)
• Functional Keywords: mcr-1, colistin, antibiotic resistance, transferase
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 36488.33

Authors

Hinchliffe, P.,Coates, K.,Walsh, T.R.,Spencer, J. (deposition date: 2017-01-22, release date: 2017-08-09, Last modification date: 2024-10-23)

Primary citation

Coates, K.,Walsh, T.R.,Spencer, J.,Hinchliffe, P.
1.12 angstrom resolution crystal structure of the catalytic domain of the plasmid-mediated colistin resistance determinant MCR-2.
Acta Crystallogr F Struct Biol Commun, 73:443-449, 2017

PubMed 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.

PubMed: 28777086
DOI: 10.1107/S2053230X17009669

Experimental method

X-RAY DIFFRACTION (1.12 Å)