Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/54375
Title: 1H- and 15N-NMR assignment and solution structure of the chemotactic Escherichia coli Che Y protein
Authors: Bruix, M., Pascual, Jaime, Santoro, Jorge, Prieto, Jestk, Serrano, Luis, Rico, Manuel
Issue Date: 1993
Publisher: Wiley-Blackwell
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. and 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.
URI: http://hdl.handle.net/10261/54375
Identifiers: doi: 10.1111/j.1432-1033.1993.tb18068.x
issn: 0014-2956
Citation: European Journal of Biochemistry 215(3): 573- 585 (1993)
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