Crystal structures of CheY mutants Y106W and T87I/Y106W. CheY activation correlates with movement of residue 106
about
Correlated switch binding and signaling in bacterial chemotaxisCrystal structure of activated CheY. Comparison with other activated receiver domainsA distinct meta-active conformation in the 1.1-A resolution structure of wild-type ApoCheYCrystal structure of a cyanobacterial phytochrome response regulatorCrystallographic and biochemical studies of DivK reveal novel features of an essential response regulator in Caulobacter crescentusThe X-ray Crystal Structures of Two Constitutively Active Mutants of the Escherichia coli PhoB Receiver Domain Give Insights into ActivationCrystal Structure of a Complex between the Phosphorelay Protein YPD1 and the Response Regulator Domain of SLN1 Bound to a Phosphoryl AnalogThe structures of T87I phosphono-CheY and T87I/Y106W phosphono-CheY help to explain their binding affinities to the FliM and CheZ peptidesConformational barrier of CheY3 and inability of CheY4 to bind FliM control the flagellar motor action in Vibrio choleraeAn asymmetric heterodomain interface stabilizes a response regulator–DNA complexUncoupled phosphorylation and activation in bacterial chemotaxis. The 2.3 A structure of an aspartate to lysine mutant at position 13 of CheYStructure of the CheY-binding domain of histidine kinase CheA in complex with CheYStructural basis for methylesterase CheB regulation by a phosphorylation-activated domainTwo binding modes reveal flexibility in kinase/response regulator interactions in the bacterial chemotaxis pathwayThe structural basis of signal transduction for the response regulator PrrA from Mycobacterium tuberculosisA network of molecular switches controls the activation of the two-component response regulator NtrC.Transcriptome analysis reveals response regulator SO2426-mediated gene expression in Shewanella oneidensis MR-1 under chromate challengeProposed signal transduction role for conserved CheY residue Thr87, a member of the response regulator active-site quintet.How signals are heard during bacterial chemotaxis: protein-protein interactions in sensory signal propagation.Conformational changes of Spo0F along the phosphotransfer pathway.Diversity in chemotaxis mechanisms among the bacteria and archaea.Probing Mechanistic Similarities between Response Regulator Signaling Proteins and Haloacid Dehalogenase Phosphatases.Structure of the Response Regulator NsrR from Streptococcus agalactiae, Which Is Involved in Lantibiotic Resistance.Acetylation at Lys-92 enhances signaling by the chemotaxis response regulator protein CheY.Genetic analysis of response regulator activation in bacterial chemotaxis suggests an intermolecular mechanism.Crystal structures of beryllium fluoride-free and beryllium fluoride-bound CheY in complex with the conserved C-terminal peptide of CheZ reveal dual binding modes specific to CheY conformation.Activation mechanism of a signaling protein at atomic resolution from advanced computationsFocus on phosphoaspartate and phosphoglutamate.Molecular dynamics of the FixJ receiver domain: movement of the beta4-alpha4 loop correlates with the in and out flip of Phe101.A new perspective on response regulator activation.Topological frustration in beta alpha-repeat proteins: sequence diversity modulates the conserved folding mechanisms of alpha/beta/alpha sandwich proteins.Biochemical study of multiple CheY response regulators of the chemotactic pathway of Rhodobacter sphaeroides.Identification of communication networks in Spo0F: a model for phosphorylation-induced conformational change and implications for activation of multiple domain bacterial response regulators.Insights into correlated motions and long-range interactions in CheY derived from molecular dynamics simulations.Subdomain competition, cooperativity, and topological frustration in the folding of CheY.Evidence against the "Y-T coupling" mechanism of activation in the response regulator NtrC.Millisecond-timescale motions contribute to the function of the bacterial response regulator protein Spo0F
P2860
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P2860
Crystal structures of CheY mutants Y106W and T87I/Y106W. CheY activation correlates with movement of residue 106
description
1997 nî lūn-bûn
@nan
1997 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
name
Crystal structures of CheY mut ...... s with movement of residue 106
@ast
Crystal structures of CheY mut ...... s with movement of residue 106
@en
Crystal structures of CheY mut ...... s with movement of residue 106
@nl
type
label
Crystal structures of CheY mut ...... s with movement of residue 106
@ast
Crystal structures of CheY mut ...... s with movement of residue 106
@en
Crystal structures of CheY mut ...... s with movement of residue 106
@nl
prefLabel
Crystal structures of CheY mut ...... s with movement of residue 106
@ast
Crystal structures of CheY mut ...... s with movement of residue 106
@en
Crystal structures of CheY mut ...... s with movement of residue 106
@nl
P2093
P2860
P356
P1476
Crystal structures of CheY mut ...... s with movement of residue 106
@en
P2093
P2860
P304
P356
10.1074/JBC.272.8.5000
P407
P577
1997-02-21T00:00:00Z