大肠杆菌P4 FliC蛋白结构分析及同源建模  

Structure Analysis and Homology Modeling of FliC from Escherichia coli P4

作　　者：李任峰[1] 田香勤[2] 何启盖[3] 胡建和[1] 赵坤[1] 李学斌[1] 王三虎[1] 

机构地区：[1]河南科技学院动物科学学院,新乡453003 [2]新乡医学院医学研究中心,新乡453003 [3]华中农业大学动物医学院农业微生物学国家重点实验室动物病原分室,武汉430070

出　　处：《生物技术通报》2010年第10期143-148,共6页Biotechnology Bulletin

基　　金：河南省基础与前沿技术研究项目(082300430020);河南科技学院青年创新基金项目(20065053)

摘　　要：为了进一步认识大肠杆菌鞭毛蛋白(Escherichia coliFliC)的结构及功能,深入研究细菌鞭毛的生物学特性,采用生物信息学方法,对组成Escherichia coliP4 FliC蛋白质的理化性质、二级结构及三级结构等进行生物信息学分析,并在三级结构的基础上进行同源建模。理化性质分析结果表明,E.coliP4 FliC蛋白为酸性结构蛋白,与沙门氏菌鞭毛蛋白性质较为接近,二级结构以α-螺旋和随机卷曲为主要构件,其空间结构与Salmonella typhimurium的3a5xA蛋白相似性较高,以此为模板成功构建了可靠的三维结构分子模型。FliC蛋白为多种细菌的鞭毛蛋白,与细菌的运动功能关系密切,本研究为深入研究细菌的运动机制及致病机理奠定基础。The research was to lucubrate bionomics of flagellin of bacteria. The amino acid sequence of FliC from Escherichia coli P4 was selected from NCBI, and analyzed by the tools of bioinformatics in the following aspects,including the composition of amino acid sequences, molecular structure,physical and chemical characters, secondary and tertiary structure of protein. Results showed that the E. coli P4 FliC was an acidic structure protein,which was similar with flagellin of Salmonella,α-helix and random coil were main compo- nent of all secondary structures. The 3D models of P4 FliC were constructed based on the template of 3aSxA by homology modeling. The flagellin is related to motility of bacteria, supporting that it would be a promising candidate for further research on the mechanism of bacteria motility and nosogenesis.

关 键 词：大肠杆菌 鞭毛蛋白 同源建模 

分 类 号：Q936[生物学—微生物学]