1eay
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(New page: 200px<br /><applet load="1eay" size="450" color="white" frame="true" align="right" spinBox="true" caption="1eay, resolution 2.0Å" /> '''CHEY-BINDING (P2) DOM...)
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Revision as of 11:45, 20 November 2007
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CHEY-BINDING (P2) DOMAIN OF CHEA IN COMPLEX WITH CHEY FROM ESCHERICHIA COLI
Overview
The crystal structure at 2.0-A resolution of the complex of the, Escherichia coli chemotaxis response regulator CheY and the, phosphoacceptor-binding domain (P2) of the kinase CheA is presented. The, binding interface involves the fourth and fifth helices and fifth, beta-strand of CheY and both helices of P2. Surprisingly, the two, heterodimers in the asymmetric unit have two different binding modes, involving the same interface, suggesting some flexibility in the binding, regions. Significant conformational changes have occurred in CheY compared, with previously determined unbound structures. The active site of CheY is, exposed by the binding of the kinase domain, possibly to enhance, phosphotransfer from CheA to CheY. The conformational changes upon complex, formation as well as the observation that there are two different binding, modes suggest that the plasticity of CheY is an essential feature of, response regulator function.
About this Structure
1EAY is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Two binding modes reveal flexibility in kinase/response regulator interactions in the bacterial chemotaxis pathway., McEvoy MM, Hausrath AC, Randolph GB, Remington SJ, Dahlquist FW, Proc Natl Acad Sci U S A. 1998 Jun 23;95(13):7333-8. PMID:9636149
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