Structural Analysis of the Domain Interface in DrrB, a Response Regulator of the OmpR/PhoB Subfamily
about
Structural basis of activity and allosteric control of diguanylate cyclaseProkaryotic 2-component systems and the OmpR/PhoB superfamilyStructure and dynamics of polymyxin-resistance-associated response regulator PmrA in complex with promoter DNAThe X-ray Crystal Structures of Two Constitutively Active Mutants of the Escherichia coli PhoB Receiver Domain Give Insights into ActivationStructure of the response regulator VicR DNA-binding domainDomain Orientation in the Inactive Response Regulator Mycobacterium tuberculosis MtrA Provides a Barrier to Activation † , ‡Crystal Structures of the Receiver Domain of the Response Regulator PhoP from Escherichia coli in the Absence and Presence of the Phosphoryl Analog BeryllofluorideThe structure of a full-length response regulator from Mycobacterium tuberculosis in a stabilized three-dimensional domain-swapped, activated stateStructure of the DNA-Binding Domain of the Response Regulator PhoP from Mycobacterium tuberculosis † , ‡Crystal Structures of the Response Regulator DosR from Mycobacterium tuberculosis Suggest a Helix Rearrangement Mechanism for Phosphorylation Activation'Hot' macromolecular crystals.Regulation of Response Regulator Autophosphorylation through Interdomain ContactsStructure of the Response Regulator PhoP from Mycobacterium tuberculosis Reveals a Dimer through the Receiver DomainStructural insights into the regulatory mechanism of the response regulator RocR from Pseudomonas aeruginosa in cyclic Di-GMP signaling.The dimeric form of the unphosphorylated response regulator BaeRSolution structure and tandem DNA recognition of the C-terminal effector domain of PmrA from Klebsiella pneumoniaeStructural insights into the dimerization of the response regulator ComE from Streptococcus pneumoniaeAtypical Response Regulator ChxR from Chlamydia trachomatis Is Structurally Poised for DNA BindingAtypical OmpR/PhoB Subfamily Response Regulator GlnR of Actinomycetes Functions as a Homodimer, Stabilized by the Unphosphorylated Conserved Asp-focused Charge InteractionsStructure of the DNA-binding domain of the response regulator SaeR from Staphylococcus aureusThe structural basis of signal transduction for the response regulator PrrA from Mycobacterium tuberculosisGenes regulated by TorR, the trimethylamine oxide response regulator of Shewanella oneidensis.A structural model of the E. coli PhoB dimer in the transcription initiation complex.Structural classification of bacterial response regulators: diversity of output domains and domain combinations.The receiver domain of hybrid histidine kinase VirA: an enhancing factor for vir gene expression in Agrobacterium tumefaciens.Regulation of the AbrA1/A2 two-component system in Streptomyces coelicolor and the potential of its deletion strain as a heterologous host for antibiotic production.Conformational Dynamics of Response Regulator RegX3 from Mycobacterium tuberculosis.Structure of the Response Regulator NsrR from Streptococcus agalactiae, Which Is Involved in Lantibiotic Resistance.PhoP-PhoP interaction at adjacent PhoP binding sites is influenced by protein phosphorylationA common dimerization interface in bacterial response regulators KdpE and TorR.Bacterial response regulators: versatile regulatory strategies from common domains.Activation of the global gene regulator PrrA (RegA) from Rhodobacter sphaeroides.Mechanism of activation for transcription factor PhoB suggested by different modes of dimerization in the inactive and active statesStructural analysis and solution studies of the activated regulatory domain of the response regulator ArcA: a symmetric dimer mediated by the alpha4-beta5-alpha5 face.Transcriptional activation by Bacillus subtilis ResD: tandem binding to target elements and phosphorylation-dependent and -independent transcriptional activation.Structural analysis of the DNA-binding domain of the Helicobacter pylori response regulator ArsR.Probing the roles of the two different dimers mediated by the receiver domain of the response regulator PhoB.In different organisms, the mode of interaction between two signaling proteins is not necessarily conserved.Biological insights from structures of two-component proteins.Molecular strategies for phosphorylation-mediated regulation of response regulator activity.
P2860
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P2860
Structural Analysis of the Domain Interface in DrrB, a Response Regulator of the OmpR/PhoB Subfamily
description
2003 nî lūn-bûn
@nan
2003 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Structural Analysis of the Dom ...... tor of the OmpR/PhoB Subfamily
@ast
Structural Analysis of the Dom ...... tor of the OmpR/PhoB Subfamily
@en
Structural Analysis of the Dom ...... tor of the OmpR/PhoB Subfamily
@nl
type
label
Structural Analysis of the Dom ...... tor of the OmpR/PhoB Subfamily
@ast
Structural Analysis of the Dom ...... tor of the OmpR/PhoB Subfamily
@en
Structural Analysis of the Dom ...... tor of the OmpR/PhoB Subfamily
@nl
prefLabel
Structural Analysis of the Dom ...... tor of the OmpR/PhoB Subfamily
@ast
Structural Analysis of the Dom ...... tor of the OmpR/PhoB Subfamily
@en
Structural Analysis of the Dom ...... tor of the OmpR/PhoB Subfamily
@nl
P2860
P1476
Structural Analysis of the Dom ...... tor of the OmpR/PhoB Subfamily
@en
P2093
Victoria L Robinson
P2860
P304
P356
10.1128/JB.185.14.4186-4194.2003
P407
P50
P577
2003-07-01T00:00:00Z