PMID:15741343

Citation	Lowery, TJ, Doucleff, M, Ruiz, EJ, Rubin, SM, Pines, A and Wemmer, DE (2005) Distinguishing multiple chemotaxis Y protein conformations with laser-polarized 129Xe NMR. Protein Sci. 14:848-55
Abstract	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.
Links	PubMed PMC2253452 Online version:10.1110/ps.041231005
Keywords	Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; Binding Sites; Crystallography, X-Ray; Lasers; Membrane Proteins/chemistry; Membrane Proteins/metabolism; Models, Molecular; Molecular Probes; Nuclear Magnetic Resonance, Biomolecular; Protein Conformation; Xenon Isotopes/chemistry; Xenon Isotopes/metabolism
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