1ZDM
Crystal Structure of Activated CheY Bound to Xe
Summary for 1ZDM
Entry DOI | 10.2210/pdb1zdm/pdb |
Related | 1DJM 1F4V 1FQW |
Descriptor | Chemotaxis protein cheY, MANGANESE (II) ION, XENON, ... (4 entities in total) |
Functional Keywords | xenon binding, protein cavities, protein conformation assay, activated chey, response regulators, bef3, signaling protein |
Biological source | Escherichia coli |
Cellular location | Cytoplasm: P06143 |
Total number of polymer chains | 2 |
Total formula weight | 28727.13 |
Authors | Lowery, T.J.,Doucleff, M.,Ruiz, E.J.,Rubin, S.M.,Pines, A.,Wemmer, D.E. (deposition date: 2005-04-14, release date: 2005-04-26, Last modification date: 2024-11-06) |
Primary citation | Lowery, T.J.,Doucleff, M.,Ruiz, E.J.,Rubin, S.M.,Pines, A.,Wemmer, D.E. Distinguishing multiple chemotaxis Y protein conformations with laser-polarized 129Xe NMR. Protein Sci., 14:848-855, 2005 Cited by PubMed Abstract: 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. PubMed: 15741343DOI: 10.1110/ps.041231005 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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