1H- and 15N-NMR assignment and solution structure of the chemotactic Escherichia coli Che Y protein.
Che Y is a 129-residue parallel alpha/beta protein involved in bacterial chemotaxis. We have used this protein as a model to study the folding reaction of parallel alpha/beta proteins. As a first step we carried out the complete assignment of the 1H and 15N spectra from Escherichia coli Che Y protein on the basis of two-dimensional 1H homonuclear and 1H-15N heteronuclear experiments by using sequence-specific methods. Our assignments differ from the preliminary assignments made by Kar et al. [Kar, L., Matsumura, P. & Johnson, M.E. (1992) Biochem. J. 287, 521-531] of aromatic residues obtained by comparison of NOEs with short proton-proton distances in the crystal structure of Che Y. The analysis of the extension of the secondary elements, as well as a preliminary calculation of the three-dimensional structure, indicate that the solution structure is closely coincident with the single crystal structure determined by X-ray diffraction.
Bruix
M
M
Instituto de Estructura de la Materia, CSIC, Madrid, Spain.
Pascual
J
J
Santoro
J
J
Prieto
J
J
Serrano
L
L
Rico
M
M
D000595:Amino Acid Sequence; D001426:Bacterial Proteins; D001483:Base Sequence; D002630:Chemotactic Factors / Q000737:chemistry*; D004277:DNA, Single-Stranded; D004926:Escherichia coli / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D008565:Membrane Proteins / Q000737:chemistry*; D000072236:Methyl-Accepting Chemotaxis Proteins; D008969:Molecular Sequence Data; D009587:Nitrogen Isotopes; D017433:Protein Structure, Secondary; D012996:Solutions; D014316:Tritium
D001426:Bacterial Proteins; D002630:Chemotactic Factors; D004277:DNA, Single-Stranded; D008565:Membrane Proteins; D000072236:Methyl-Accepting Chemotaxis Proteins; D009587:Nitrogen Isotopes; D012996:Solutions; D014316:Tritium