Distinguishing multiple chemotaxis Y protein conformations with laser-polarized 129Xe NMR.
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.
Lowery
Thomas J
TJ
Physical Biosciences Divisions, Lawrence Berkeley National Laboratory, 1 Cyclotron Road, Berkeley, CA 94720, USA.
Doucleff
Michaeleen
M
Ruiz
E Janette
EJ
Rubin
Seth M
SM
Pines
Alexander
A
Wemmer
David E
DE
D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D001665:Binding Sites; D018360:Crystallography, X-Ray; D029968:Escherichia coli Proteins; D007834:Lasers; D008565:Membrane Proteins / Q000737:chemistry* / Q000378:metabolism; D000072236:Methyl-Accepting Chemotaxis Proteins; D008958:Models, Molecular; D015335:Molecular Probes; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation; D014979:Xenon Isotopes / Q000737:chemistry* / Q000378:metabolism
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D008565:Membrane Proteins; D000072236:Methyl-Accepting Chemotaxis Proteins; D015335:Molecular Probes; D014979:Xenon Isotopes; C000607606:cheY protein, E coli
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