The contact interface of a 120 kD CheA-CheW complex by methyl TROSY interaction spectroscopy.
During bacterial chemotaxis, the histidine autokinase CheA interacts with the chemotaxis receptors with the help of the coupling protein CheW. This interaction is typical of many macromolecular complexes where protein-protein interactions play an important role. In this case, a relatively small protein, CheW, becomes part of a much larger complex. Here we describe a new method to map the residues at a protein-protein interface for macromolecular complexes of molecular weight greater than 100 kD.
Department of Chemistry and Biochemistry, University of California Santa Barbara, California 93106, USA.
Damon J
DJ
Hamel
Frederick W
FW
Dahlquist
D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism*; D001665:Binding Sites; D009682:Magnetic Resonance Spectroscopy; D008565:Membrane Proteins / Q000737:chemistry* / Q000378:metabolism*; D000072236:Methyl-Accepting Chemotaxis Proteins; D008745:Methylation; D008958:Models, Molecular; D008970:Molecular Weight; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D020124:Thermotoga maritima
D001426:Bacterial Proteins; D008565:Membrane Proteins; D000072236:Methyl-Accepting Chemotaxis Proteins; C051236:CheW protein, Bacteria