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

TitleDistinguishing multiple chemotaxis Y protein conformations with laser-polarized Xe-129 NMR
Publication TypeJournal Article
Year of Publication2005
AuthorsLowery T.J, Doucleff M., Ruiz E.J, Rubin S.M, Pines A, Wemmer D.E
JournalProtein Science
Volume14
Issue4
Pagination848-855
Date PublishedApr
ISBN Number0961-8368
Accession NumberWOS:000227738900002
Keywordscavity
Abstract

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

URL<Go to ISI>://WOS:000227738900002
DOI10.1110/Ps.041231005
Short TitleDistinguishing multiple chemotaxis Y protein conformations with laser-polarized Xe-129 NMR
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