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Distinguishing multiple chemotaxis Y protein conformations with laser-polarized 129Xe NMR.

Thomas J TJ Lowery, Michaeleen M Doucleff, E Janette EJ Ruiz, Seth M SM Rubin, Alexander A Pines, and David E DE Wemmer

Protein Sci 14(4):848-55 (2005) PMID 15741343 PMCID 2253452

The chemical shift of the (129)Xe NMR signal has been shown to be extremely sensitive to the local environment around the atom and has been used to follow processes such as ligand binding by bacterial periplasmic binding proteins. Here we show that the (129)Xe shift can sense more subtle changes: magnesium binding, BeF(3)(-) activation, and peptide binding by the Escherichia coli chemotaxis Y protein. (1)H-(15)N correlation spectroscopy and X-ray crystallography were used to identify two xenon-binding cavities in CheY that are primarily responsible for the shift changes. One site is near the active site, and the other is near the peptide binding site.

DOI: 10.1110/ps.041231005
Version: za2963e q8zad q8zb1 q8zca q8zd4 q8zea q8zfc q8zg8

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