Structure of a conserved receptor domain that regulates kinase activity: the cytoplasmic domain of bacterial taxis receptors
Structure of a conserved receptor domain that regulates kinase activity: the cytoplasmic domain of bacterial taxis receptors
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DOI：
10.1016/s0959-440x(00)00115-9
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发表时间：
2000-08-01
影响因子：
6.8
通讯作者：
Kim, SH
中科院分区：
文献类型：
--
作者：
Falke, JJ;Kim, SH
许多细菌是能动的，并使用一类保守的跨膜感觉受体来调节细胞向最佳生存环境的趋化性。这些保守的受体通常由细胞外信号刺激，但也通过在其胞质结构域上的特定位点处的共价修饰进行适应。胞质结构域的功能是整合细胞外信号和适应性信号，并利用这种整合的信息来调节相关的组氨酸激酶。激酶，反过来，触发细胞质磷酸化途径的两个组件类。最近已确定的高分辨率结构的受体胞质结构域的结晶学方法，并在很大程度上是一致的结构模型独立产生的化学研究的域中的全长，膜结合受体。这些结果代表了一个重要的一步，对受体激酶的信息传递机制的理解。
Many bacteria are motile and use a conserved class of transmembrane sensory receptor to regulate cellular taxis toward an optimal living environment. These conserved receptors are typically stimulated by extracellular signals, but also undergo adaptation via covalent modification at specific sites on their cytoplasmic domains. The function of the cytoplasmic domain is to integrate the extracellular and adaptive signals, and to use this integrated information to regulate an associated histidine kinase. The kinase, in turn, triggers a cytoplasmic phosphorylation pathway of the two-component class. The high-resolution structure of a receptor cytoplasmic domain has recently been determined by crystallographic methods and is largely consistent with a structural model independently generated by chemical studies of the domain in the full-length, membrane-bound receptor. These results represent an important step toward a mechanistic understanding of receptor-to-kinase information transfer.