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Distinguishing multiple chemotaxis Y protein conformations with laser‐polarized 129 Xe NMR
Author(s) -
Lowery Thomas J.,
Doucleff Michaeleen,
Ruiz E. Janette,
Rubin Seth M.,
Pines Alexander,
Wemmer David E.
Publication year - 2005
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.041231005
Subject(s) - periplasmic space , chemotaxis , chemistry , nuclear magnetic resonance spectroscopy , binding site , peptide , escherichia coli , ligand (biochemistry) , chemical shift , biophysics , crystallography , stereochemistry , biochemistry , biology , receptor , gene
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.