Crystal structure of a full-length LysR-type transcriptional regulator, CbnR: unusual combination of two subunit forms and molecular bases for causing and changing DNA bend
about
Modulating DNA bending affects NodD-mediated transcriptional control in Rhizobium leguminosarum.CbbR, the Master Regulator for Microbial Carbon Dioxide FixationTranscription factor-based biosensors enlightened by the analyteThe Subtleties and Contrasts of the LeuO Regulator in Salmonella Typhi: Implications in the Immune ResponseOligomerization of BenM, a LysR-type transcriptional regulator: structural basis for the aggregation of proteins in this familyStructures of open (R) and close (T) states of prephenate dehydratase (PDT)—Implication of allosteric regulation by l-phenylalanineThe structure of CrgA from Neisseria meningitidis reveals a new octameric assembly state for LysR transcriptional regulatorsThe structure of a reduced form of OxyR from Neisseria meningitidisCrystal structures of DntR inducer binding domains in complex with salicylate offer insights into the activation of LysR-type transcriptional regulatorsStructure of the regulatory domain of the LysR family regulator NMB2055 (MetR-like protein) fromNeisseria meningitidisThe crystal structure of AphB, a virulence gene activator from Vibrio cholerae, reveals residues that influence its response to oxygen and pHCrystal Structures of the LsrR Proteins Complexed with Phospho-AI-2 and Two Signal-Interrupting Analogues Reveal Distinct Mechanisms for Ligand RecognitionStructures of thePorphyromonas gingivalisOxyR regulatory domain explain differences in expression of the OxyR regulon inEscherichia coliandP. gingivalisThe DNA-binding domain of BenM reveals the structural basis for the recognition of a T-N11-A sequence motif by LysR-type transcriptional regulatorsMolecular mechanism of the regulation of Bacillus subtilis gltAB expression by GltCThe mycobacterial LysR-type regulator OxyS responds to oxidative stress and negatively regulates expression of the catalase-peroxidase gene.High crystallizability under air-exclusion conditions of the full-length LysR-type transcriptional regulator TsaR from Comamonas testosteroni T-2 and data-set analysis for a MIRAS structure-solution approach.Structural classification of bacterial response regulators: diversity of output domains and domain combinations.Detection of and response to signals involved in host-microbe interactions by plant-associated bacteria.Specificity of the E. coli LysR-type transcriptional regulators.Structure of lambda CII: implications for recognition of direct-repeat DNA by an unusual tetrameric organizationA LysR-type regulator, CidR, is required for induction of the Staphylococcus aureus cidABC operonRegulatory system of the protocatechuate 4,5-cleavage pathway genes essential for lignin downstream catabolism.Lactobacillus brevis responds to flavonoids through KaeR, a LysR-type of transcriptional regulator.Factors that influence the response of the LysR type transcriptional regulators to aromatic compounds.Genetic analysis of the nitrogen assimilation control protein from Klebsiella pneumoniae.The LysR-type nitrogen assimilation control protein forms complexes with both long and short DNA binding sites in the absence of coeffectors.Properties of the NAC (nitrogen assimilation control protein)-binding site within the ureD promoter of Klebsiella pneumoniae.Importance of tetramer formation by the nitrogen assimilation control protein for strong repression of glutamate dehydrogenase formation in Klebsiella pneumoniaeCcpC-dependent regulation of citB and lmo0847 in Listeria monocytogenes.The LysR-type transcriptional regulator VirR is required for expression of the virulence gene vapA of Rhodococcus equi ATCC 33701CatM regulation of the benABCDE operon: functional divergence of two LysR-type paralogs in Acinetobacter baylyi ADP1.Structural and functional characterization of Pseudomonas aeruginosa global regulator AmpR.Transcriptional activation of multiple operons involved in para-nitrophenol degradation by Pseudomonas sp. Strain WBC-3The β-lactamase gene regulator AmpR is a tetramer that recognizes and binds the D-Ala-D-Ala motif of its repressor UDP-N-acetylmuramic acid (MurNAc)-pentapeptideThe cation-responsive protein NhaR of Escherichia coli activates pgaABCD transcription, required for production of the biofilm adhesin poly-beta-1,6-N-acetyl-D-glucosamine.Mutational analysis to define an activating region on the redox-sensitive transcriptional regulator OxyR.Most mutant OccR proteins that are defective in positive control hold operator DNA in a locked high-angle bend.Intra-chain 3D segment swapping spawns the evolution of new multidomain protein architectures.The control of death and lysis in staphylococcal biofilms: a coordination of physiological signals
P2860
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P2860
Crystal structure of a full-length LysR-type transcriptional regulator, CbnR: unusual combination of two subunit forms and molecular bases for causing and changing DNA bend
description
2003 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի մայիսին հրատարակված գիտական հոդված
@hy
article scientifique (publié 2003/05/02)
@fr
articolo scientifico (pubblicato il 2003/05/02)
@it
artigo científico (publicado na 2003/05/02)
@pt
artículu científicu espublizáu en 2003
@ast
im Mai 2003 veröffentlichter wissenschaftlicher Artikel
@de
scientific article (publication date: 2 May 2003)
@en
vedecký článok (publikovaný 2003/05/02)
@sk
videnskabelig artikel (udgivet 2003/05/02)
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name
Crystal structure of a full-le ...... causing and changing DNA bend
@ast
Crystal structure of a full-le ...... causing and changing DNA bend
@en
Crystal structure of a full-le ...... causing and changing DNA bend
@nl
type
label
Crystal structure of a full-le ...... causing and changing DNA bend
@ast
Crystal structure of a full-le ...... causing and changing DNA bend
@en
Crystal structure of a full-le ...... causing and changing DNA bend
@nl
prefLabel
Crystal structure of a full-le ...... causing and changing DNA bend
@ast
Crystal structure of a full-le ...... causing and changing DNA bend
@en
Crystal structure of a full-le ...... causing and changing DNA bend
@nl
P2093
P1476
Crystal structure of a full-le ...... causing and changing DNA bend
@en
P2093
Kiyotaka Miyashita
Naoto Ogawa
Rumi Okumura
Shin Muraoka
Takamasa Nonaka
P304
P356
10.1016/S0022-2836(03)00312-7
P407
P577
2003-05-01T00:00:00Z