Authors: Cho HS, Lee SY, Yan D, Pan X, Parkinson JS, Kustu S, Wemmer DE, Pelton JG
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.
[NMR paper] NMR backbone assignment of the mitogen-activated protein (MAP) kinase p38.
NMR backbone assignment of the mitogen-activated protein (MAP) kinase p38.
Related Articles NMR backbone assignment of the mitogen-activated protein (MAP) kinase p38.
J Biomol NMR. 2005 Jun;32(2):175
Authors: Vogtherr M, Saxena K, Grimme S, Betz M, Schieborr U, Pescatore B, Langer T, Schwalbe H
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[NMR paper] An NMR view of the folding process of a CheY mutant at the residue level.
An NMR view of the folding process of a CheY mutant at the residue level.
Related Articles An NMR view of the folding process of a CheY mutant at the residue level.
Structure. 2002 Sep;10(9):1173-1185
Authors: Garcia P, Serrano L, Rico M, Bruix M
The folding of CheY mutant F14N/V83T was studied at 75 residues by NMR. Fluorescence, NMR, and sedimentation equilibrium studies at different urea and protein concentrations reveal that the urea-induced unfolding of this CheY mutant includes an on-pathway molten globule-like intermediate that can...
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[NMR paper] NMR and SAXS characterization of the denatured state of the chemotactic protein CheY:
NMR and SAXS characterization of the denatured state of the chemotactic protein CheY: implications for protein folding initiation.
Related Articles NMR and SAXS characterization of the denatured state of the chemotactic protein CheY: implications for protein folding initiation.
Protein Sci. 2001 Jun;10(6):1100-12
Authors: Garcia P, Serrano L, Durand D, Rico M, Bruix M
The denatured state of a double mutant of the chemotactic protein CheY (F14N/V83T) has been analyzed in the presence of 5 M urea, using small angle X-ray scattering (SAXS) and...
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[NMR paper] Activation of the phosphosignaling protein CheY. II. Analysis of activated mutants by
Activation of the phosphosignaling protein CheY. II. Analysis of activated mutants by 19F NMR and protein engineering.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc-MS.gif Related Articles Activation of the phosphosignaling protein CheY. II. Analysis of activated mutants by 19F NMR and protein engineering.
J Biol Chem. 1993 Jun 25;268(18):13089-96
Authors: Bourret RB, Drake SK, Chervitz SA, Simon MI, Falke JJ
The Escherichia coli CheY protein is activated by phosphorylation,...
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[NMR paper] Activation of the phosphosignaling protein CheY. I. Analysis of the phosphorylated co
Activation of the phosphosignaling protein CheY. I. Analysis of the phosphorylated conformation by 19F NMR and protein engineering.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc-MS.gif Related Articles Activation of the phosphosignaling protein CheY. I. Analysis of the phosphorylated conformation by 19F NMR and protein engineering.
J Biol Chem. 1993 Jun 25;268(18):13081-8
Authors: Drake SK, Bourret RB, Luck LA, Simon MI, Falke JJ
CheY, the 14-kDa response regulator protein of...
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[NMR paper] Biophysical investigations on L1210 mouse leukemia cells treated with activated cyclo
Biophysical investigations on L1210 mouse leukemia cells treated with activated cyclophosphamide metabolites: determination of selective properties of DNA-interstrand and DNA-protein cross-linking mechanisms (alkaline elution and 31P-NMR-spectroscopy) and some aspects of the combination drug and radiotherapy.
Related Articles Biophysical investigations on L1210 mouse leukemia cells treated with activated cyclophosphamide metabolites: determination of selective properties of DNA-interstrand and DNA-protein cross-linking mechanisms (alkaline elution and 31P-NMR-spectroscopy) and...
NMR structure of activated CheY.
Linear Mode
