1a0o
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(New page: 200px<br /><applet load="1a0o" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a0o, resolution 2.95Å" /> '''CHEY-BINDING DOMAIN ...)
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Revision as of 08:24, 20 November 2007
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CHEY-BINDING DOMAIN OF CHEA IN COMPLEX WITH CHEY
Overview
Bacterial adaptation to the environment is accomplished through the, coordinated activation of specific sensory receptors and signal processing, proteins. Among the best characterized of these pathways are those which, employ the two-component paradigm. In these systems, signal transmission, is mediated by Mg(2+)-dependent phospho-relay reactions between histidine, auto-kinases and phospho-accepting receiver domains in response-regulator, proteins. Although this mechanism of activation is common to all, response-regulators, detrimental cross-talk between different, two-component pathways within the same cell is minimized through the use, of specific recognition domains. Here, we report the crystal structure, at, 2.95 A resolution, of the response regulator of bacterial chemotaxis, CheY, bound to the recognition domain from its cognate histidine kinase, CheA. The structure suggests that molecular recognition, in this low, affinity complex (KD = 2 microM), may also contribute to the mechanism of, CheY activation.
About this Structure
1A0O is a Protein complex structure of sequences from Escherichia coli with MN as ligand. Full crystallographic information is available from OCA.
Reference
Structure of the CheY-binding domain of histidine kinase CheA in complex with CheY., Welch M, Chinardet N, Mourey L, Birck C, Samama JP, Nat Struct Biol. 1998 Jan;5(1):25-9. PMID:9437425
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