The CheZ binding interface of CheAS is located in alpha-helix E.
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.
O'Connor
Christopher
C
Department of Microbiology and Immunology, College of Medicine, University of Illinois at Chicago, Chicago, Illinois 60612, USA.
Matsumura
Philip
P
Campos
Andres
A
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
D001426:Bacterial Proteins; D008565:Membrane Proteins; D000072236:Methyl-Accepting Chemotaxis Proteins