PMID:10731410

Citation	Cho, HS, Lee, SY, Yan, D, Pan, X, Parkinson, JS, Kustu, S, Wemmer, DE and Pelton, JG (2000) NMR structure of activated CheY. J. Mol. Biol. 297:543-51
Abstract	The CheY protein is the response regulator in bacterial chemotaxis. Phosphorylation of a conserved aspartyl residue induces structural changes that convert the protein from an inactive to an active state. The short half-life of the aspartyl-phosphate has precluded detailed structural analysis of the active protein. Persistent activation of Escherichia coli CheY was achieved by complexation with beryllofluoride (BeF(3)(-)) and the structure determined by NMR spectroscopy to a backbone r.m.s.d. of 0.58(+/-0.08) A. Formation of a hydrogen bond between the Thr87 OH group and an active site acceptor, presumably Asp57.BeF(3)(-), stabilizes a coupled rearrangement of highly conserved residues, Thr87 and Tyr106, along with displacement of beta4 and H4, to yield the active state. The coupled rearrangement may be a more general mechanism for activation of receiver domains.
Links	PubMed Online version:10.1006/jmbi.2000.3595
Keywords	Amino Acid Sequence; Bacterial Proteins; Beryllium/metabolism; Beryllium/pharmacology; Binding Sites; Conserved Sequence; Enzyme Activation/drug effects; Enzyme Stability/drug effects; Escherichia coli/enzymology; Fluorides/metabolism; Fluorides/pharmacology; Hydrogen Bonding; Membrane Proteins/chemistry; Membrane Proteins/metabolism; Models, Molecular; Molecular Sequence Data; Nuclear Magnetic Resonance, Biomolecular; Phosphorylation; Protein Conformation/drug effects
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