Three-dimensional structure of CheY, the response regulator of bacterial chemotaxis
about
Histidine protein kinases: key signal transducers outside the animal kingdomKeeping signals straight in phosphorelay signal transductionBeF(3)(-) acts as a phosphate analog in proteins phosphorylated on aspartate: structure of a BeF(3)(-) complex with phosphoserine phosphataseProtein phosphorylation and regulation of adaptive responses in bacteriaIdentification of a novel response regulator required for the swarmer-to-stalked-cell transition in Caulobacter crescentusProkaryotic 2-component systems and the OmpR/PhoB superfamilyCrystal structure of a cyanobacterial phytochrome response regulatorCrystallographic and biochemical studies of DivK reveal novel features of an essential response regulator in Caulobacter crescentusMolecular basis for the local conformational rearrangement of human phosphoserine phosphataseA General Strategy to Solve the Phase Problem in RNA CrystallographyInteraction of CheY with the C-Terminal Peptide of CheZCrystal Structures of the Response Regulator DosR from Mycobacterium tuberculosis Suggest a Helix Rearrangement Mechanism for Phosphorylation ActivationA structural model of anti-anti-σ inhibition by a two-component receiver domain: the PhyR stress response regulatorStructure and binding specificity of the receiver domain of sensor histidine kinase CKI1 from Arabidopsis thalianaNuclear Magnetic Resonance Structure and Dynamics of the Response Regulator Sma0114 from Sinorhizobium melilotiConformational barrier of CheY3 and inability of CheY4 to bind FliM control the flagellar motor action in Vibrio choleraeCrystal structures of CheY mutants Y106W and T87I/Y106W. CheY activation correlates with movement of residue 106Uncoupled phosphorylation and activation in bacterial chemotaxis. The 2.3 A structure of an aspartate to lysine mutant at position 13 of CheYStructural basis for methylesterase CheB regulation by a phosphorylation-activated domainSix new candidate members of the alpha/beta twisted open-sheet family detected by sequence similarity to flavodoxin.The difficult case of crystallization and structure solution for the ParC55 breakage-reunion domain of topoisomerase IV from Streptococcus pneumoniaeA transcriptional activator, FleQ, regulates mucin adhesion and flagellar gene expression in Pseudomonas aeruginosa in a cascade mannerPhosphorylation-induced dimerization of the FixJ receiver domain.Crystal structures of two cyanobacterial response regulators in apo- and phosphorylated form reveal a novel dimerization motif of phytochrome-associated response regulators.High Resolution Structures of Periplasmic Glucose-binding Protein of Pseudomonas putida CSV86 Reveal Structural Basis of Its Substrate SpecificityStructural trees for protein superfamilies.Promoter elements required for positive control of transcription of the Escherichia coli uhpT geneStructure of a central stalk subunit F of prokaryotic V-type ATPase/synthase from Thermus thermophilusBivalent-metal binding to CheY protein. Effect on protein conformationAn ABC transporter plays a developmental aggregation role in Myxococcus xanthus.Structural classification of bacterial response regulators: diversity of output domains and domain combinations.Identification of sensory and signal-transducing domains in two-component signaling systems.FrzE of Myxococcus xanthus is homologous to both CheA and CheY of Salmonella typhimurium.Enhancement of RNA polymerase binding to promoters by a transcriptional activator, OmpR, in Escherichia coli: its positive and negative effects on transcriptionProposed signal transduction role for conserved CheY residue Thr87, a member of the response regulator active-site quintet.Interaction fidelity in two-component signaling.Phosphorylation-dependent conformational changes in OmpR, an osmoregulatory DNA-binding protein of Escherichia coli.Activation of the phosphosignaling protein CheY. II. Analysis of activated mutants by 19F NMR and protein engineeringThe two-component signaling pathway of bacterial chemotaxis: a molecular view of signal transduction by receptors, kinases, and adaptation enzymesActivation of the phosphosignaling protein CheY. I. Analysis of the phosphorylated conformation by 19F NMR and protein engineering
P2860
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P2860
Three-dimensional structure of CheY, the response regulator of bacterial chemotaxis
description
1989 nî lūn-bûn
@nan
1989 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1989 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1989年の論文
@ja
1989年論文
@yue
1989年論文
@zh-hant
1989年論文
@zh-hk
1989年論文
@zh-mo
1989年論文
@zh-tw
1989年论文
@wuu
name
Three-dimensional structure of CheY, the response regulator of bacterial chemotaxis
@ast
Three-dimensional structure of CheY, the response regulator of bacterial chemotaxis
@en
Three-dimensional structure of CheY, the response regulator of bacterial chemotaxis
@nl
type
label
Three-dimensional structure of CheY, the response regulator of bacterial chemotaxis
@ast
Three-dimensional structure of CheY, the response regulator of bacterial chemotaxis
@en
Three-dimensional structure of CheY, the response regulator of bacterial chemotaxis
@nl
prefLabel
Three-dimensional structure of CheY, the response regulator of bacterial chemotaxis
@ast
Three-dimensional structure of CheY, the response regulator of bacterial chemotaxis
@en
Three-dimensional structure of CheY, the response regulator of bacterial chemotaxis
@nl
P2093
P3181
P356
P1433
P1476
Three-dimensional structure of CheY, the response regulator of bacterial chemotaxis
@en
P2093
C E Schutt
J M Mottonen
P2888
P3181
P356
10.1038/337745A0
P407
P577
1989-02-23T00:00:00Z
P6179
1050539488