Three-dimensional structure of the diphtheria toxin repressor in complex with divalent cation co-repressors.
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Structures of the apo- and the metal ion-activated forms of the diphtheria tox repressor from Corynebacterium diphtheriaeSolution structure of the ETS domain from murine Ets-1: a winged helix-turn-helix DNA binding motifClinical microbiology of coryneform bacteriaMetal stoichiometry and functional studies of the diphtheria toxin repressorTranscription factor-based biosensors enlightened by the analyteSolution structure and peptide binding studies of the C-terminal src homology 3-like domain of the diphtheria toxin repressor proteinCrystal structure of the iron-dependent regulator from Mycobacterium tuberculosis at 2.0-A resolution reveals the Src homology domain 3-like fold and metal binding function of the third domainDeterminants of the Src Homology Domain 3-Like FoldCharacterization and Structure of the Manganese-Responsive Transcriptional Regulator ScaR ,Roles of the A and C Sites in the Manganese-Specific Activation of MntRStructural analysis and insight into metal-ion activation of the iron-dependent regulator from Thermoplasma acidophilumStructure of the metal-ion-activated diphtheria toxin repressor/tox operator complexMotion of the DNA-binding domain with respect to the core of the diphtheria toxin repressor (DtxR) revealed in the crystal structures of apo- and holo-DtxRCharacterization of an iron-dependent regulatory protein (IdeR) of Mycobacterium tuberculosis as a functional homolog of the diphtheria toxin repressor (DtxR) from Corynebacterium diphtheriaeFunctional studies of the Mycobacterium tuberculosis iron-dependent regulatorGenetic and biophysical studies of diphtheria toxin repressor (DtxR) and the hyperactive mutant DtxR(E175K) support a multistep model of activation.Isolation and characterization of iron-independent positive dominant mutants of the diphtheria toxin repressor DtxRConstruction and characterization of transposon insertion mutations in Corynebacterium diphtheriae that affect expression of the diphtheria toxin repressor (DtxR).SirR, a novel iron-dependent repressor in Staphylococcus epidermidisBiology and molecular epidemiology of diphtheria toxin and the tox gene.Disordered to ordered folding in the regulation of diphtheria toxin repressor activity.Transcriptional control of the iron-responsive fxbA gene by the mycobacterial regulator IdeR.Anion-coordinating residues at binding site 1 are essential for the biological activity of the diphtheria toxin repressor.Characterization of MtsR, a new metal regulator in group A streptococcus, involved in iron acquisition and virulence.Classification of multi-helical DNA-binding domains and application to predict the DBD structures of sigma factor, LysR, OmpR/PhoB, CENP-B, Rapl, and Xy1S/Ada/AraC.Mechanism of metal ion activation of the diphtheria toxin repressor DtxR.Analysis of a DtxR-like metalloregulatory protein, MntR, from Corynebacterium diphtheriae that controls expression of an ABC metal transporter by an Mn(2+)-dependent mechanismTranscription of the contiguous sigB, dtxR, and galE genes in Corynebacterium diphtheriae: evidence for multiple transcripts and regulation by environmental factors.The src homology 3-like domain of the diphtheria toxin repressor (DtxR) modulates repressor activation through interaction with the ancillary metal ion-binding siteIdentification and functional analysis of CT069 as a novel transcriptional regulator in ChlamydiaIdentification and characterization of three new promoter/operators from Corynebacterium diphtheriae that are regulated by the diphtheria toxin repressor (DtxR) and ironCrystallization and preliminary X-ray diffraction analysis of the metalloregulatory protein DtxR from Thermoplasma acidophilumRegulatory circuit based on autogenous activation-repression: roles of C-boxes and spacer sequences in control of the PvuII restriction-modification system.Backbone dynamics in an intramolecular prolylpeptide-SH3 complex from the diphtheria toxin repressor, DtxR.IdeR in mycobacteria: from target recognition to physiological function.Structural basis for the metal-selective activation of the manganese transport regulator of Bacillus subtilis.Treponema denticola TroR is a manganese- and iron-dependent transcriptional repressor.Analysis of genes that encode DtxR-like transcriptional regulators in pathogenic and saprophytic corynebacterial speciesAt the crossroads of bacterial metabolism and virulence factor synthesis in StaphylococciCo-crystallization of an ETS domain (PU.1) in complex with DNA. Engineering the length of both protein and oligonucleotide.
P2860
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P2860
Three-dimensional structure of the diphtheria toxin repressor in complex with divalent cation co-repressors.
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
1995年论文
@zh
1995年论文
@zh-cn
name
Three-dimensional structure of ...... divalent cation co-repressors.
@ast
Three-dimensional structure of ...... divalent cation co-repressors.
@en
type
label
Three-dimensional structure of ...... divalent cation co-repressors.
@ast
Three-dimensional structure of ...... divalent cation co-repressors.
@en
prefLabel
Three-dimensional structure of ...... divalent cation co-repressors.
@ast
Three-dimensional structure of ...... divalent cation co-repressors.
@en
P2093
P1433
P1476
Three-dimensional structure of ...... divalent cation co-repressors.
@en
P2093
P304
P356
10.1016/S0969-2126(01)00137-X
P577
1995-01-01T00:00:00Z