Crystal structure of Escherichia coli CheY refined at 1.7-A resolution
about
Use of 19F NMR to probe protein structure and conformational changesMultiple protein structure alignmentCrystal structure of a cyanobacterial phytochrome response regulatorThe crystal structure of the phosphorylation domain in PhoP reveals a functional tandem association mediated by an asymmetric interfaceCrystal structure of a phosphatase with a unique substrate binding domain fromThermotoga maritimaNMR structure of the pseudo-receiver domain of CikAThe structures of T87I phosphono-CheY and T87I/Y106W phosphono-CheY help to explain their binding affinities to the FliM and CheZ peptidesUsing Structural Information to Change the Phosphotransfer Specificity of a Two-Component Chemotaxis Signalling ComplexCrystal Structure of Activated CheY1 from Helicobacter pyloriSolution Structure of a Complex of the Histidine Autokinase CheA with Its Substrate CheYConformational barrier of CheY3 and inability of CheY4 to bind FliM control the flagellar motor action in Vibrio choleraeCrystal structure of casein kinase-1, a phosphate-directed protein kinaseStructural basis for methylesterase CheB regulation by a phosphorylation-activated domainTwo binding modes reveal flexibility in kinase/response regulator interactions in the bacterial chemotaxis pathwayPhosphorylated Ssk1 prevents unphosphorylated Ssk1 from activating the Ssk2 mitogen-activated protein kinase kinase kinase in the yeast high-osmolarity glycerol osmoregulatory pathwaySix new candidate members of the alpha/beta twisted open-sheet family detected by sequence similarity to flavodoxin.A transcriptional activator, FleQ, regulates mucin adhesion and flagellar gene expression in Pseudomonas aeruginosa in a cascade mannerBivalent-metal binding to CheY protein. Effect on protein conformationA specialized version of the HD hydrolase domain implicated in signal transductionStructural classification of bacterial response regulators: diversity of output domains and domain combinations.Emergence of protein fold families through rational designIdentification of sensory and signal-transducing domains in two-component signaling systems.Simulated diffusion of phosphorylated CheY through the cytoplasm of Escherichia coli.Contrasting roles of dynamics in protein allostery: NMR and structural studies of CheY and the third PDZ domain from PSD-95.Phosphorylation-independent activity of the response regulators AlgB and AlgR in promoting alginate biosynthesis in mucoid Pseudomonas aeruginosa.Proposed signal transduction role for conserved CheY residue Thr87, a member of the response regulator active-site quintet.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 engineeringModulation of frustration in folding by sequence permutation.The 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 engineeringThe VirR response regulator from Clostridium perfringens binds independently to two imperfect direct repeats located upstream of the pfoA promoterGenetic evidence that the alpha5 helix of the receiver domain of PhoB is involved in interdomain interactionsHow signals are heard during bacterial chemotaxis: protein-protein interactions in sensory signal propagation.Relationship between ion pair geometries and electrostatic strengths in proteins.Conferring thermostability to mesophilic proteins through optimized electrostatic surfaces.Conformational changes of Spo0F along the phosphotransfer pathway.Kinetic buffering of cross talk between bacterial two-component sensors.Diversity in chemotaxis mechanisms among the bacteria and archaea.Allosteric response is both conserved and variable across three CheY orthologs.
P2860
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P2860
Crystal structure of Escherichia coli CheY refined at 1.7-A resolution
description
1991 nî lūn-bûn
@nan
1991 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
1991 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
1991年の論文
@ja
1991年論文
@yue
1991年論文
@zh-hant
1991年論文
@zh-hk
1991年論文
@zh-mo
1991年論文
@zh-tw
1991年论文
@wuu
name
Crystal structure of Escherichia coli CheY refined at 1.7-A resolution
@ast
Crystal structure of Escherichia coli CheY refined at 1.7-A resolution
@en
Crystal structure of Escherichia coli CheY refined at 1.7-A resolution
@nl
type
label
Crystal structure of Escherichia coli CheY refined at 1.7-A resolution
@ast
Crystal structure of Escherichia coli CheY refined at 1.7-A resolution
@en
Crystal structure of Escherichia coli CheY refined at 1.7-A resolution
@nl
prefLabel
Crystal structure of Escherichia coli CheY refined at 1.7-A resolution
@ast
Crystal structure of Escherichia coli CheY refined at 1.7-A resolution
@en
Crystal structure of Escherichia coli CheY refined at 1.7-A resolution
@nl
P1476
Crystal structure of Escherichia coli CheY refined at 1.7-A resolution
@en
P2093
P304
P407
P577
1991-08-15T00:00:00Z