The solution structure and interactions of CheW from Thermotoga maritima.
Using protein from the hyperthermophile Thermotoga maritima, we have determined the solution structure of CheW, an essential component in the formation of the bacterial chemotaxis signaling complex. The overall fold is similar to the regulatory domain of the chemotaxis kinase CheA. In addition, interactions of CheW with CheA were monitored by nuclear magnetic resonance (NMR) techniques. The chemical shift perturbation data show the probable contacts that CheW makes with CheA. In combination with previous genetic data, the structure also suggests a possible binding site for the chemotaxis receptor. These results provide a structural basis for a model in which CheW acts as a molecular bridge between CheA and the cytoplasmic tails of the receptor.
Griswold
Ian J
IJ
Institute of Molecular Biology, Department of Chemistry, University of Oregon Eugene, Oregon 97403, USA.
Zhou
Hongjun
H
Matison
Mikenzie
M
Swanson
Ronald V
RV
McIntosh
Lawrence P
LP
Simon
Melvin I
MI
Dahlquist
Frederick W
FW
D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism*; D001665:Binding Sites; D002633:Chemotaxis; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism*; D000072236:Methyl-Accepting Chemotaxis Proteins; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D011485:Protein Binding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011956:Receptors, Cell Surface / Q000378:metabolism; D012996:Solutions; D013329:Structure-Activity Relationship; D020124:Thermotoga maritima / Q000737:chemistry*
D001426:Bacterial Proteins; D008565:Membrane Proteins; D000072236:Methyl-Accepting Chemotaxis Proteins; D011956:Receptors, Cell Surface; D012996:Solutions; C051236:CheW protein, Bacteria