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

¹ Department of Chemistry, University of California at Berkeley, Berkeley, California 94720, USA
² Materials Sciences and ³ Physical Biosciences Divisions, Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA

(RECEIVED November 16, 2004; FINAL REVISION January 6, 2005; ACCEPTED January 6, 2005)

The chemical shift of the ¹²⁹Xe 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 ¹²⁹Xe shift can sense more subtle changes: magnesium binding, BeF₃^– activation, and peptide binding by the Escherichia coli chemotaxis Y protein. ¹H-¹⁵N 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.

Keywords: xenon binding; CheY; protein cavities; protein conformation assay

Article published online ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.041231005.

Reprint requests to: David E. Wemmer, Physical Biosciences Divisions, Lawrence Berkeley National Laboratory, 1 Cyclotron Road, Berkeley, CA 94720, USA; e-mail: DEWemmer{at}lbl.gov; fax: (510) 486-6059.

⁴ Present address: Memorial Sloan-Kettering Cancer Center, New York, NY 10021, USA.

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