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质粒介导的黏菌素耐药决定因子MCR-2催化结构域的1.12埃分辨率晶体结构

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

作者信息

Coates Katie, Walsh Timothy R, Spencer James, Hinchliffe Philip

机构信息

School of Cellular and Molecular Medicine, University of Bristol, Bristol BS8 1TD, England.

Department of Medical Microbiology and Infectious Disease, Cardiff Institute of Infection and Immunity, UHW Main Building, Heath Park Hospital, Cardiff CF14 4XN, Wales.

出版信息

Acta Crystallogr F Struct Biol Commun. 2017 Aug 1;73(Pt 8):443-449. doi: 10.1107/S2053230X17009669. Epub 2017 Jul 26.

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.

摘要

MCR-2赋予对黏菌素的抗性,黏菌素是一种针对广泛耐药革兰氏阴性病原体的“最后一道防线”抗生素。它是一种质粒编码的磷酸乙醇胺转移酶,与MCR-1密切相关。为了解MCR家族的多样性,测定了MCR-2催化结构域分辨率为1.12 Å的晶体结构。可变氨基酸位于远离双锌活性位点和膜近端表面的位置。这一超高分辨率将为进一步的机制研究提供一个精确的起始模型。

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