1u0s

Chemotaxis kinase CheA P2 domain in complex with response regulator CheY from the thermophile thermotoga maritima

spinqualitylabelsall models 1u0s, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1u0s is a 2 chain structure with sequence from Thermotoga maritima. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.9Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CHEY_THEMA Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. CheY seems to regulate the clockwise (CW) rotation (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Although interfaces mediating protein-protein interactions are thought to be under strong evolutionary constraints, binding of the chemotaxis histidine kinase CheA to its phosphorylation target CheY suggests otherwise. The structure of Thermotoga maritima CheA domain P2 in complex with CheY reveals a different association than that observed for the same Escherichia coli proteins. Similar regions of CheY bind CheA P2 in the two systems, but the CheA P2 domains differ by an approximately 90 degrees rotation. CheA binds CheY with identical affinity in T. maritima and E. coli at the vastly different temperatures where the respective organisms live. Distinct sets of P2 residues mediate CheY binding in the two complexes; conservation patterns of these residues in CheA and compensations in CheY delineate two families of prokaryotic chemotaxis systems. A protein complex that has the same components and general function in different organisms, but an altered structure, indicates unanticipated complexity in the evolution of protein-protein interactions and cautions against extrapolating structural data from homologs. In different organisms, the mode of interaction between two signaling proteins is not necessarily conserved.,Park SY, Beel BD, Simon MI, Bilwes AM, Crane BR Proc Natl Acad Sci U S A. 2004 Aug 10;101(32):11646-51. Epub 2004 Aug 2. PMID:15289606 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Chemotaxis protein 3D structures

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