Structure of the metal-ion-activated diphtheria toxin repressor/tox operator complex
about
The solution structure of the Zalpha domain of the human RNA editing enzyme ADAR1 reveals a prepositioned binding surface for Z-DNAMetal stoichiometry and functional studies of the diphtheria toxin repressorTranscription factor-based biosensors enlightened by the analyteRelaxosome function and conjugation regulation in F-like plasmids - a structural biology perspectiveThe high-resolution crystal structure of the molybdate-dependent transcriptional regulator (ModE) from Escherichia coli: a novel combination of domain foldsSolution 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 domainCorepressor-induced organization and assembly of the biotin repressor: A model for allosteric activation of a transcriptional regulatorStructural basis for cooperative DNA binding by two dimers of the multidrug-binding protein QacRDeterminants of the Src Homology Domain 3-Like FoldThree-dimensional structure of MecI. Molecular basis for transcriptional regulation of staphylococcal methicillin resistanceCharacterization and Structure of the Manganese-Responsive Transcriptional Regulator ScaR ,Structural basis of cooperative DNA recognition by the plasmid conjugation factor, TraMA winged helix domain in human MUS81 binds DNA and modulates the endonuclease activity of MUS81 complexesPoint mutations in Helicobacter pylori's fur regulatory gene that alter resistance to metronidazole, a prodrug activated by chemical reductionFunctional studies of the Mycobacterium tuberculosis iron-dependent regulatorThe Mycobacterium tuberculosis IdeR is a dual functional regulator that controls transcription of genes involved in iron acquisition, iron storage and survival in macrophagesRecognition of DNA by Fur: a reinterpretation of the Fur box consensus sequence.Genetic 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 DtxRStructure solution of DNA-binding proteins and complexes with ARCIMBOLDO libraries.Mechanistic insights into metal ion activation and operator recognition by the ferric uptake regulator.Human MUS81-EME2 can cleave a variety of DNA structures including intact Holliday junction and nicked duplex.Dynamic equilibrium on DNA defines transcriptional regulation of a multidrug binding transcriptional repressor, LmrR.Opening the iron box: transcriptional metalloregulation by the Fur protein.The response of Pseudomonas aeruginosa to iron: genetics, biochemistry and virulence.Biology and molecular epidemiology of diphtheria toxin and the tox gene.Boosting the prediction and understanding of DNA-binding domains from sequenceDisordered to ordered folding in the regulation of diphtheria toxin repressor activity.Cd(II)-responsive and constitutive mutants implicate a novel domain in MerR.Anion-coordinating residues at binding site 1 are essential for the biological activity of the diphtheria toxin repressor.Dual repression by Fe(2+)-Fur and Mn(2+)-MntR of the mntH gene, encoding an NRAMP-like Mn(2+) transporter in Escherichia coli.Both Corynebacterium diphtheriae DtxR(E175K) and Mycobacterium tuberculosis IdeR(D177K) are dominant positive repressors of IdeR-regulated genes in M. tuberculosis.A structural-alphabet-based strategy for finding structural motifs across protein families.Geobacter uraniireducens NikR displays a DNA binding mode distinct from other members of the NikR family.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 mechanismComponents of the ligand for a Ni++ reactive human T cell clone.A quantitative measure of electrostatic perturbation in holo and apo enzymes induced by structural changesArchitecture of a fur binding site: a comparative analysis
P2860
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P2860
Structure of the metal-ion-activated diphtheria toxin repressor/tox operator complex
description
1998 nî lūn-bûn
@nan
1998 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Structure of the metal-ion-activated diphtheria toxin repressor/tox operator complex
@ast
Structure of the metal-ion-activated diphtheria toxin repressor/tox operator complex
@en
Structure of the metal-ion-activated diphtheria toxin repressor/tox operator complex
@nl
type
label
Structure of the metal-ion-activated diphtheria toxin repressor/tox operator complex
@ast
Structure of the metal-ion-activated diphtheria toxin repressor/tox operator complex
@en
Structure of the metal-ion-activated diphtheria toxin repressor/tox operator complex
@nl
prefLabel
Structure of the metal-ion-activated diphtheria toxin repressor/tox operator complex
@ast
Structure of the metal-ion-activated diphtheria toxin repressor/tox operator complex
@en
Structure of the metal-ion-activated diphtheria toxin repressor/tox operator complex
@nl
P2093
P2860
P356
P1433
P1476
Structure of the metal-ion-activated diphtheria toxin repressor/tox operator complex
@en
P2093
P2860
P2888
P356
10.1038/28893
P407
P50
P577
1998-07-30T00:00:00Z
P6179
1001083573