结核分枝杆菌酰基辅酶A脱氢酶的晶体学初步研究  

Preliminary Crystallographic Studies of An Acyl-CoA-dehydrogenase(Rv0244c)from Mycobacterium Tuberculosis

作　　者：陈晓博 陈佳玥 周卫红[1] Chen Xiaobo;Chen Jiayue;Zhou Weihong(College of Life Sciences,Nankai University,Tianjin 300071,China)

机构地区：[1]南开大学生命科学学院,天津300071

出　　处：《南开大学学报（自然科学版）》2021年第5期76-81,共6页Acta Scientiarum Naturalium Universitatis Nankaiensis

基　　金：国家重点研发项目(152017YFC0840300)。

摘　　要：结核病是人类健康的重要威胁.随着多药耐药和广泛耐药结核分枝杆菌菌株,以及结核分枝杆菌与人类免疫缺陷病毒共感染现象的出现,寻找新的更安全有效的药物靶标迫在眉睫.对来自结核分枝杆菌的潜在药物靶标进行蛋白三维结构的阐释是研究抗结核药物的有力手段之一.酰基辅酶A脱氢酶在结核分枝杆菌的脂肪酸合成酶系统中发挥着重要的作用,有可能成为潜在的药物靶标.在大肠杆菌中克隆表达了酰基辅酶A脱氢酶蛋白FadE5,经多步蛋白质的纯化和结晶条件的筛选后,获得具有衍射能力的蛋白质晶体,并收集了分辨率为0.29 nm的X-射线衍射数据.这些实验和衍射数据都为FadE5蛋白的晶体结构与功能的研究奠定了基础.M.tuberculosis is an serious threat to human health.With the emergence of co-infection with M.tuberculosis and human immunodeficiency virus(HIV),finding new safer and more effective drug targets is imminent.One of the powerful tool for anti-TB drug discovery is to elucidate the 3 D structures of potential drug targets from M.tuberculosis.Acyl-Co A dehydrogenase plays an important role in the fatty acid synthase system of M.tuberculosis and was proved to be associated with drug resistance.In this paper,acyl-CoA dehydrogenase Fad E5 was expressed in Escherichia coli,purified and screened by multiple methods to obtain single crystals.X-ray diffraction data of the protein crystal with a resolution of 0.29 nm was collected and processed.All these data laid the foundation for the structure and function study of the FadE5 protein.

关 键 词：结核分枝杆菌 酰基辅酶A脱氢酶 FadE5 蛋白质晶体 

分 类 号：Q71[生物学—分子生物学]