Structural highlights
Function
A0A1C3NEV1_ECOLX
Publication Abstract from PubMed
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 A 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.
1.12 A resolution crystal structure of the catalytic domain of the plasmid-mediated colistin resistance determinant MCR-2.,Coates K, Walsh TR, Spencer J, Hinchliffe P Acta Crystallogr F Struct Biol Commun. 2017 Aug 1;73(Pt 8):443-449. doi:, 10.1107/S2053230X17009669. Epub 2017 Jul 26. PMID:28777086[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Coates K, Walsh TR, Spencer J, Hinchliffe P. 1.12 A resolution crystal structure of the catalytic domain of the plasmid-mediated colistin resistance determinant MCR-2. Acta Crystallogr F Struct Biol Commun. 2017 Aug 1;73(Pt 8):443-449. doi:, 10.1107/S2053230X17009669. Epub 2017 Jul 26. PMID:28777086 doi:http://dx.doi.org/10.1107/S2053230X17009669