Crystal structure of cytotoxin protein suilysin from Streptococcus suis

作     者：Lingfeng Xu Bo Huang Huamao Du Xuejun CZhang Jianguo Xu Xuemei Li Zihe Rao 

作者机构：National Laboratory of BiomacromoleculesInstitute of BiophysicsChinese Academy of Sciences15 Datun RoadBeijing 100101China College of BiotechnologySouthwest UniversityChongqing 400715China State Key Laboratory for Infectious Disease Prevention and ControlNational Institute for Communicable Disease Control and PreventionBeijing 102200China Protein Studies ProgramOklahoma Medical Research Foundation825 N.E.13th streetOklahoma CityOK 73104USA 

出 版 物：《Protein & Cell》 (蛋白质与细胞（英文版）)

年 卷 期：2010年第1卷第1期

页      面：96-105页

核心收录：

学科分类：1002[医学-临床医学] 10[医学] 

基　　金：This work was supported by the National Programs for High Technology Research and Development Program(863 Program)No.2006AA02A322 to X.L.,the CAS grant KSCX2-YW-05 to Z.R,the Project of Protein Studies(CAS)grant 2006CB10903 National Basic Research Program(973 Program)No.2007CB914304 

主　　题：suilysin cholesterol-dependent cytolysin crystal structure 

摘      要：Cholesterol-dependent cytolysins(CDC)are pore forming toxins.A prototype of the CDC family members is perfringolysin O(PFO),which directly binds to the cell membrane enriched in cholesterol,causing cell ***,an exception of this general observation is intermedilysin(ILY)of Streptococcus intermedius,which requires human CD59 as a receptor in addition to cholesterol for its hemolytic activity.A possible explanation of this functional difference is the conformational variation between the C-terminal domains of the two toxins,particularly in the highly conserved undecapeptide termed tryptophan rich ***,we present the crystal structure of suilysin,a CDC toxin from the infectious swine pathogen Streptococcus *** PFO,suilysin does not require a host receptor for hemolytic activity;yet the crystal structure of suilysin exhibits a similar conformation in the tryptophan rich motif to *** observation suggests that the current view of the structure-function relationship between CDC proteins and membrane association is far from complete.