1H‐ and15N‐NMR assignment and solution structure of the chemotacticEscherichia coliChe Y protein

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Abstract
Che Y is a 129‐residue parallel α/β protein involved in bacterial chemotaxis. We have used this protein as a model to study the folding reaction of parallel α/β 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.

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