Structure of CheA, a signal-transducing histidine kinase
Structure of CheA, a signal-transducing histidine kinase
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DOI：
10.1016/s0092-8674(00)80966-6
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发表时间：
1999-01-08
期刊：
影响因子：
64.5
通讯作者：
Simon, MI
中科院分区：
文献类型：
--
作者：
Bilwes, AM;Alex, LA;Simon, MI
组氨酸激酶使细菌、植物和真菌能够感知环境并对其做出反应。海栖热袍菌 CheA (290-671) 组氨酸激酶的 2.6 埃分辨率晶体结构揭示了二聚体，其中二聚化、ATP 结合和调节的功能被隔离在多个域中。该激酶结构域与 Ser/Thr/Tyr 激酶不同，但类似于两种 ATP 酶：促旋酶 B 和 Hsp90。该超家族内的结构类比表明 CheA 的 P1 结构域为磷酸转移提供亲核组氨酸和活化谷氨酸。结合同源受体偶联蛋白 CheW 的调节结构域在拓扑上类似于两个 SH3 结构域，并在两端提供不同的蛋白质识别表面。二聚化结构域形成一个中心四螺旋束，激酶和调节结构域围绕该四螺旋束以保守铰链为枢轴以调节转磷酸化。不同的亚基构象表明相对结构域运动将受体响应与激酶活性联系起来。
Histidine kinases allow bacteria, plants, and fungi to sense and respond to their environment. The 2.6 Angstrom resolution crystal structure of Thermotoga maritima CheA (290-671) histidine kinase reveals a dimer where the functions of dimerization, ATP binding, and regulation are segregated into domains. The kinase domain is unlike Ser/Thr/Tyr kinases but resembles two ATPases, Gyrase B and Hsp90. Structural analogies within this superfamily suggest that the P1 domain of CheA provides the nucleophilic histidine and activating glutamate for phosphotransfer. The regulatory domain, which binds the homologous receptor-coupling protein CheW, topologically resembles two SH3 domains and provides different protein recognition surfaces at each end. The dimerization domain forms a central four-helix bundle about which the kinase and regulatory domains pivot on conserved hinges to modulate transphosphorylation. Different subunit conformations suggest that relative domain motions link receptor response to kinase activity.