title: The CheZ binding interface of CheAS is located in alpha-helix E.
abstract: 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. Both L123 and L126 are buried in CheA-long (CheA(L)), providing an explanation for why CheA(L) fails to bind CheZ.
authors: Department of Microbiology and Immunology, College of Medicine, University of Illinois at Chicago, Chicago, Illinois 60612, USA.
authors: Christopher
authors: C
authors: O'Connor
authors: Philip
authors: P
authors: Matsumura
authors: Andres
authors: A
authors: Campos
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D001665:Binding Sites; D002633:Chemotaxis; D015964:Gene Expression Regulation, Bacterial; D009682:Magnetic Resonance Spectroscopy; D008565:Membrane Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D000072236:Methyl-Accepting Chemotaxis Proteins; D008958:Models, Molecular; D009154:Mutation; D017433:Protein Structure, Secondary; D015398:Signal Transduction
chemical_list: D001426:Bacterial Proteins; D008565:Membrane Proteins; D000072236:Methyl-Accepting Chemotaxis Proteins