2ch4 | pdb_00002ch4

Complex between Bacterial Chemotaxis histidine kinase CheA domains P4 and P5 and receptor-adaptor protein CheW

spinqualitylabelsall models 2ch4, resolution 3.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2ch4 is a 4 chain structure with sequence from Atcc 43589. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ANP Related: 1b3q, 1i58, 1i59, 1i5a, 1i5b, 1i5c, 1i5d, 1tqg, 1u0s, 1k0s Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [CHEW_THEMA] Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors (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 In bacterial chemotaxis, an assembly of transmembrane receptors, the CheA histidine kinase and the adaptor protein CheW processes environmental stimuli to regulate motility. The structure of a Thermotoga maritima receptor cytoplasmic domain defines CheA interaction regions and metal ion-coordinating charge centers that undergo chemical modification to tune receptor response. Dimeric CheA-CheW, defined by crystallography and pulsed ESR, positions two CheWs to form a cleft that is lined with residues important for receptor interactions and sized to clamp one receptor dimer. CheW residues involved in kinase activation map to interfaces that orient the CheW clamps. CheA regulatory domains associate in crystals through conserved hydrophobic surfaces. Such CheA self-contacts align the CheW receptor clamps for binding receptor tips. Linking layers of ternary complexes with close-packed receptors generates a lattice with reasonable component ratios, cooperative interactions among receptors and accessible sites for modification enzymes. Reconstruction of the chemotaxis receptor-kinase assembly.,Park SY, Borbat PP, Gonzalez-Bonet G, Bhatnagar J, Pollard AM, Freed JH, Bilwes AM, Crane BR Nat Struct Mol Biol. 2006 May;13(5):400-7. Epub 2006 Apr 23. PMID:16622408 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Acetylcholinesterase 3D structures Chemotaxis protein

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