|Title||Distinguishing multiple chemotaxis Y protein conformations with laser-polarized Xe-129 NMR|
|Publication Type||Journal Article|
|Year of Publication||2005|
|Authors||Lowery T.J, Doucleff M., Ruiz E.J, Rubin S.M, Pines A, Wemmer D.E|
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|
|Short Title||Distinguishing multiple chemotaxis Y protein conformations with laser-polarized Xe-129 NMR|
Distinguishing multiple chemotaxis Y protein conformations with laser-polarized Xe-129 NMR