3-DIMENSIONAL STRUCTURE OF CHEY, THE RESPONSE REGULATOR OF BACTERIAL CHEMOTAXIS
3-DIMENSIONAL STRUCTURE OF CHEY, THE RESPONSE REGULATOR OF BACTERIAL CHEMOTAXIS
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DOI：
10.1038/337745a0
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发表时间：
1989-02-23
期刊：
影响因子：
64.8
通讯作者：
SCHUTT, CE
中科院分区：
文献类型：
--
作者：
STOCK, AM;MOTTONEN, JM;SCHUTT, CE
细菌信号转导蛋白之间的同源性表明，共同的机制介导诸如趋化性、细菌调节、孢子形成、毒力以及对氮、磷和氧剥夺的响应的过程1 -3。最近在趋化性、氮调节和细胞周期调节中鉴定了一种常见的激酶介导的磷酸转移反应4 -10。在趋化性中，CheA激酶将磷酰基传递到胞质蛋白CheY，其作为磷酸化激活的开关与鞭毛组分相互作用以调节运动性。本文报道了鼠伤寒沙门氏菌CheY蛋白的X射线晶体结构。通过使用位点特异性诱变来工程化重原子结合位点来促进结构的测定。CheY是一种单结构域蛋白，由一个双缠绕的五链平行β折叠组成。CheY中的磷酸受体位点可能是β折叠的C末端边缘附近的天冬氨酸侧链簇。CheY与其他调控系统组分的序列相似性模式可以根据CheY结构来解释，并支持这一蛋白质家族具有共同结构基序和活性位点的观点。
Homologies among bacterial signal transduction proteins suggest that a common mechanism mediates processes such as chemotaxis, osmoregulation, sporulation, virulence, and responses to nitrogen, phosphorous and oxygen deprivation1–3. A common kinase-mediated phosphotransfer reaction has recently been identified in chemotaxis, nitrogen regulation, and osmoregulation4–10. In chemotaxis, the CheA kinase passes a phosphoryl group to the cytoplasmic protein CheY, which functions as a phosphorylation-activated switch that interacts with flagellar components to regulate motility. We report here the X-ray crystal structure of theSalmonella typhimuriumCheY protein. The determination of the structure was facilitated by the use of site-specific mutagenesis to engineer heavy-atom binding sites. CheY is a single-domain protein composed of a doubly wound five-stranded parallelβ-sheet. The phosphoacceptor site in CheY is probably a cluster of aspartic-acid side chains near the C-terminal edge of theβ-sheet. The pattern of sequence similarity of CheY with components of other regulatory systems can be interpreted in the light of the CheY structure and supports the view that this family of proteins have a common structural motif and active site.