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Published online before print March 1, 2005, 10.1110/ps.041231005
Protein Science (2005), 14:848-855. Published by Cold Spring Harbor Laboratory Press. Copyright © 2005 The Protein Society
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Distinguishing multiple chemotaxis Y protein conformations with laser-polarized 129Xe NMR

Thomas J. Lowery1,3, Michaeleen Doucleff1,3, E. Janette Ruiz1,2, Seth M. Rubin1,3,4, Alexander Pines1,2 and David E. Wemmer1,3

1 Department of Chemistry, University of California at Berkeley, Berkeley, California 94720, USA2 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)

Abstract

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.


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