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1ZDM

Crystal Structure of Activated CheY Bound to Xe

Summary for 1ZDM
Entry DOI10.2210/pdb1zdm/pdb
Related1DJM 1F4V 1FQW
DescriptorChemotaxis protein cheY, MANGANESE (II) ION, XENON, ... (4 entities in total)
Functional Keywordsxenon binding, protein cavities, protein conformation assay, activated chey, response regulators, bef3, signaling protein
Biological sourceEscherichia coli
Cellular locationCytoplasm: P06143
Total number of polymer chains2
Total formula weight28727.13
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 citationLowery, 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: 15741343
DOI: 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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