Solution structure of a complex of the histidine autokinase CheA with its substrate CheY.
Solution structure of a complex of the histidine autokinase CheA with its substrate CheY.
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DOI：
10.1021/bi300147m
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发表时间：
2012-05-08
期刊：
影响因子：
2.9
通讯作者：
Dahlquist FW
中科院分区：
文献类型：
--
作者：
Mo G;Zhou H;Kawamura T;Dahlquist FW
In bacterial chemotaxis two-component signaling system, the histidine-containing phosphotransfer domain (the “P1” domain) of CheA receives a phosphoryl group from the catalytic domain (P4) of CheA and transfers it to the cognate response regulator (RR) CheY, which is docked by the P2 domain of CheA. Phosphorylated CheY then diffuses in cytoplasm and interacts with the FliM moiety of the flagellar motors, thereby modulating the direction of the flagella rotation. Structures of various histidine phosphotransfer domains (HPt) complexed with their cognate RR domain have been reported. Unlike the E. coli chemotaxis system, however, these systems lack the additional domains dedicated to binding to the response regulators, and the interaction of an HPt domain with an RR in the presence of such a domain has not been examined on the structural basis. In this study, we used modern NMR techniques to construct a model for the interaction of the E. coli CheA P1 domain (HPt) and CheY (RR) in the presence of the CheY-binding domain, P2. Our results indicate that the presence of P2 may lead to a slightly different relative orientation of the HPt and RR domains from those seen in such complex structures previously reported.
