文献类型： 外文期刊
作者： Liu, Zhao-Xin 1 ; Han, Zhenggang 1 ; Yu, Xiao-Li 1 ; Wen, Guoyuan 3 ; Zeng, Chi 1 ;
作者机构： 1.Wuhan Polytech Univ, Sch Biol & Pharmaceut Engn, Hubei Prov Engn Res Ctr Hlth Food, Wuhan 430023, Hubei, Peoples R China
2.Wuhan Univ, Coll Life Sci, Wuhan 430072, Hubei, Peoples R China
3.Hubei Acad Agr Sci, Inst Anim Husb & Vet, Key Lab Prevent & Control Agents Anim Bacteriosis, Minist Agr, Wuhan 430064, Hubei, Peoples R China
关键词： polymyxin resistance; colistin resistance; MCR-1
期刊名称：CRYSTALS （ 影响因子：2.589； 五年影响因子：2.615 ）
ISSN： 2073-4352
年卷期： 2018 年 8 卷 4 期
页码：
收录情况： SCI
摘要： The polymyxin colistin is known as a "last resort" antibacterial drug toward pandrug-resistant enterobacteria. The recently discovered plasmid-encoded mcr-1 gene spreads rapidly across pathogenic strains and confers resistance to colistin, which has emerged as a global threat. The mcr-1 gene encodes a phosphoethanolamine transferase (MCR-1) that catalyzes the transference of phosphoethanolamine to lipid A moiety of lipopolysaccharide, resulting in resistance to colistin. Development of effective MCR-1 inhibitors is crucial for combating MCR-1-mediated colistin resistance. In this study, MCR-1 catalytic domain (namely cMCR-1) was expressed and co-crystallized together with D-xylose. X-ray crystallographic study at a resolution of 1.8 angstrom found that cMCR-1-d-xylose co-crystals fell under space group P2(1)2(1)2(1), with unit-cell parameters a = 51.6 angstrom, b = 73.1 angstrom, c = 82.2 angstrom, alpha = 90 degrees, beta = 90 degrees, gamma = 90 degrees. The asymmetric unit contained a single cMCR-1 molecule complexed with d-xylose and had a solvent content of 29.13%. The structural model of cMCR-1-d-xylose complex showed that a D-xylose molecule bound in the putative lipid A-binding pocket of cMCR-1, which might provide a clue for MCR-1 inhibitor development.
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