Crystal structure of the protease-resistant core domain of Yersinia pestis virulence factor YopR.
Crystal structure of the protease-resistant core domain of Yersinia pestis virulence factor YopR.
复制标题
鼠疫耶尔森氏菌毒力因子 YopR 的蛋白酶抗性核心结构域的晶体结构。
DOI：
10.1110/ps.051446405
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发表时间：
2005
期刊：
影响因子：
--
通讯作者：
Waugh,DavidS
中科院分区：
文献类型：
--
作者：
Schubot,FlorianD;Cherry,Scott;Austin,BrianP;Tropea,JosephE;Waugh,DavidS
Yersinia pestis, the causative agent of the plague, employs a type III secretion system (T3SS) to secrete and translocate virulence factors into to the cytoplasm of mammalian host cells. One of the secreted virulence factors is YopR. Little is known about the function of YopR other than that it is secreted into the extracellular milieu during the early stages of infection and that it contributes to virulence. Hoping to gain some insight into the function of YopR, we determined the crystal structure of its protease‐resistant core domain, which consists of residues 38–149 out of 165 amino acids. The core domain is composed of five α‐helices that display unexpected structural similarity with one domain of YopN, a central regulator of type III secretion inY. pestis. This finding raises the possibility that YopR may play a role in the regulation of type III secretion.
