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- W2154030500 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." @default.
- W2154030500 created "2016-06-24" @default.
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- W2154030500 date "2000-03-01" @default.
- W2154030500 modified "2023-10-06" @default.
- W2154030500 title "NMR structure of activated CheY" @default.
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- W2154030500 doi "https://doi.org/10.1006/jmbi.2000.3595" @default.
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