Distinguishing multiple chemotaxis Y protein conformations with laser-polarized 129Xe NMR
The chemical shift of the {sup 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 (Rubin et al. 2000; Lowery et al. 2004). Here we show that the {sup 129}Xe shift can sense more subtle changes: magnesium binding, BeF{sub 3}{sup -} activation, and peptide binding by the E. coli chemotaxis Y protein. {sup 1}H-{sup 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.
- Research Organization:
- Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States)
- Sponsoring Organization:
- USDOE. Laboratory Directed Research and Development Program; Office of Naval Research DMI-II, National Science Foundation; Lucent Technologies/Bell Laboratories Predoctoral Fellowship (US)
- DOE Contract Number:
- AC03-76SF00098
- OSTI ID:
- 841325
- Report Number(s):
- LBNL-56980; R&D Project: 366420; TRN: US200513%%590
- Journal Information:
- Protein Science, Vol. 14, Issue 4; Other Information: Submitted to Protein Science: Volume 14, No.4; Journal Publication Date: 04/2005; PBD: 1 Feb 2005
- Country of Publication:
- United States
- Language:
- English
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