1A0O

CHEY-BINDING DOMAIN OF CHEA IN COMPLEX WITH CHEY

Summary for 1A0O

• Entry DOI: 10.2210/pdb1a0o/pdb
• Descriptor: CHEY, CHEA, MANGANESE (II) ION (3 entities in total)
• Functional Keywords: bacterial chemotaxis, signal transduction, two-component system, histidine kinase, response regulator, chemotaxis
• Biological source: Escherichia coli; More
• Cellular location: Cytoplasm: P07363
• Total number of polymer chains: 8
• Total formula weight: 114165.80

Authors

Chinardet, N.,Welch, M.,Mourey, L.,Birck, C.,Samama, J.P. (deposition date: 1997-12-05, release date: 1998-12-30, Last modification date: 2024-05-22)

Primary citation

Welch, M.,Chinardet, N.,Mourey, L.,Birck, C.,Samama, J.P.
Structure of the CheY-binding domain of histidine kinase CheA in complex with CheY.
Nat.Struct.Biol., 5:25-29, 1998

PubMed Abstract: 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.

PubMed: 9437425
DOI: 10.1038/nsb0198-25

Experimental method

X-RAY DIFFRACTION (2.95 Å)