cheA Antibody

1. Signaling complexes control CheA by altering its apparent rate constant of autophosphorylation. PMID: 28425142
2. Differences were observed, however, in a keel-like density that we identify here as CheA kinase domains P1 and P2, the phosphorylation site domain and the binding domain for response regulator target proteins. PMID: 23802570
3. Thus, these P1 phosphorylation domain mutants appear to define interaction determinants for P1-P4 docking during the CheA autophosphorylation reaction. PMID: 24163342
4. crystal of CheA belonged to space group P1, with unit-cell parameters a = 59.271, b = 67.674, c = 82.815 A, alpha = 77.568, beta = 86.073, gamma = 64.436 degrees . The asymmetric unit may contain up to ten dimeric units of P3 four-helix bundles PMID: 21636905
5. The fluorescence properties of CheA carrying a Phe455Trp replacement can be used to monitor ATP-binding events and a conformational change at the CheA protein histidine kinase active site. PMID: 15766267
6. Results describe the ranges and kinetics of domain motions in the free CheA dimer. PMID: 19256549
7. Specific CheA-short (CheA(S)) residues, L123 and L126, were identified as critical for CheZ binding. In the CheA(S) 'P1-CheZ nuclear magnetic resonance structure, these residues form an interaction surface on alpha-helix E in the 'P1 domain. PMID: 19581362

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KEGG: ecj:JW1877

STRING: 316407.1736547