The structure of the cofactor-binding fragment of the LysR family member, CysB: a familiar fold with a surprising subunit arrangement
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Modulating DNA bending affects NodD-mediated transcriptional control in Rhizobium leguminosarum.CbbR, the Master Regulator for Microbial Carbon Dioxide FixationThe high-resolution crystal structure of the molybdate-dependent transcriptional regulator (ModE) from Escherichia coli: a novel combination of domain foldsOligomerization of BenM, a LysR-type transcriptional regulator: structural basis for the aggregation of proteins in this familyThe 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 regulatorsThe DNA-binding domain of BenM reveals the structural basis for the recognition of a T-N11-A sequence motif by LysR-type transcriptional regulatorsInsights from the architecture of the bacterial transcription apparatusDiverse flavonoids stimulate NodD1 binding to nod gene promoters in Sinorhizobium meliloti.Functional insights from structural predictions: analysis of the Escherichia coli genome.MEDS and PocR are novel domains with a predicted role in sensing simple hydrocarbon derivatives in prokaryotic signal transduction systems.The signaling helix: a common functional theme in diverse signaling proteins.Regulation of benzoate degradation in Acinetobacter sp. strain ADP1 by BenM, a LysR-type transcriptional activator.Detection of and response to signals involved in host-microbe interactions by plant-associated bacteria.Specificity of the E. coli LysR-type transcriptional regulators.The amino-terminal 100 residues of the nitrogen assimilation control protein (NAC) encode all known properties of NAC from Klebsiella aerogenes and Escherichia coliFactors that influence the response of the LysR type transcriptional regulators to aromatic compounds.Genetic analysis of the nitrogen assimilation control protein from Klebsiella pneumoniae.Proteins with similar architecture exhibit similar large-scale dynamic behavior.Tetrapyrrole biosynthesis in Rhodobacter capsulatus is transcriptionally regulated by the heme-binding regulatory protein, HbrL.Isolation of a negative control mutant of the nitrogen assimilation control protein, NAC, in Klebsiella aerogenesCharacterization of TsaR, an oxygen-sensitive LysR-type regulator for the degradation of p-toluenesulfonate in Comamonas testosteroni T-2The 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.Most mutant OccR proteins that are defective in positive control hold operator DNA in a locked high-angle bend.Benzoate decreases the binding of cis,cis-muconate to the BenM regulator despite the synergistic effect of both compounds on transcriptional activation.Interaction of serine acetyltransferase with O-acetylserine sulfhydrylase active site: evidence from fluorescence spectroscopyIsolation and characterization of mutant Sinorhizobium meliloti NodD1 proteins with altered responses to luteolinFunctional dissection of the LysR-type CysB transcriptional regulator. Regions important for DNA binding, inducer response, oligomerization, and positive control.An updated structural classification of substrate-binding proteins.Isolation and characterization of mutations in the Escherichia coli regulatory protein XapRThe structure of full-length LysR-type transcriptional regulators. Modeling of the full-length OxyR transcription factor dimer.Inactivation of the nod box distal half-site allows tetrameric NodD to activate nodA transcription in an inducer-independent manner.Origins of coevolution between residues distant in protein 3D structures.Crystallization and preliminary X-ray analysis of CrgA, a LysR-type transcriptional regulator from pathogenic Neisseria meningitidis MC58Purification, crystallization and preliminary X-ray diffraction analysis of the C-terminal fragment of the MvfR protein from Pseudomonas aeruginosa.Constitutive mutations of the OccR regulatory protein affect DNA bending in response to metabolites released from plant tumors.The switch from inorganic to organic sulphur assimilation in Escherichia coli: adenosine 5'-phosphosulphate (APS) as a signalling molecule for sulphate excess.Residues that influence in vivo and in vitro CbbR function in Rhodobacter sphaeroides and identification of a specific region critical for co-inducer recognition.Amino acid residues critical for DNA binding and inducer recognition in CbnR, a LysR-type transcriptional regulator from Cupriavidus necator NH9.
P2860
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P2860
The structure of the cofactor-binding fragment of the LysR family member, CysB: a familiar fold with a surprising subunit arrangement
description
1997 nî lūn-bûn
@nan
1997 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի օգոստոսին 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
The structure of the cofactor- ...... surprising subunit arrangement
@ast
The structure of the cofactor- ...... surprising subunit arrangement
@en
The structure of the cofactor- ...... surprising subunit arrangement
@nl
type
label
The structure of the cofactor- ...... surprising subunit arrangement
@ast
The structure of the cofactor- ...... surprising subunit arrangement
@en
The structure of the cofactor- ...... surprising subunit arrangement
@nl
prefLabel
The structure of the cofactor- ...... surprising subunit arrangement
@ast
The structure of the cofactor- ...... surprising subunit arrangement
@en
The structure of the cofactor- ...... surprising subunit arrangement
@nl
P2093
P1433
P1476
The structure of the cofactor- ...... surprising subunit arrangement
@en
P2093
A J Wilkinson
E J Dodson
G N Murshudov
K H Verschueren
P304
P356
10.1016/S0969-2126(97)00254-2
P577
1997-08-15T00:00:00Z