1.12 Å resolution crystal structure of the catalytic domain of the plasmid-mediated colistin resistance determinant MCR-2.
1.12 Å resolution crystal structure of the catalytic domain of the plasmid-mediated colistin resistance determinant MCR-2.
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DOI：
10.1107/s2053230x17009669
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发表时间：
2017-08-01
期刊：
影响因子：
--
通讯作者：
Hinchliffe P
中科院分区：
文献类型：
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作者：
Coates K;Walsh TR;Spencer J;Hinchliffe P
质粒介导的粘菌素抗性决定子 MCR-2 的晶体结构已在 1.12 Å 分辨率下测定。这种高分辨率结构突出了临床相关 MCR 蛋白的分子多样性，并为进一步的机械研究，特别是计算研究提供了准确的起始模型。 MCR-2 赋予粘菌素耐药性，粘菌素是针对广泛耐药的革兰氏阴性病原体的“最后一线”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。为了了解 MCR 家族的多样性，确定了 MCR-2 催化结构域的 1.12 Å 分辨率晶体结构。可变氨基酸位于远离二锌活性位点和膜近端面的位置。极高的分辨率将为进一步的机理研究提供准确的起始模型。
The crystal structure of the plasmid-mediated colistin resistance determinant MCR-2 has been determined at 1.12 Å resolution. This high-resolution structure highlights the molecular diversity of clinically relevant MCR proteins and provides an accurate starting model for further mechanistic, and in particular computational, studies. 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.