Escherichia coli biotin holoenzyme synthetase/bio repressor crystal structure delineates the biotin- and DNA-binding domains
about
The N-terminal domain of human holocarboxylase synthetase facilitates biotinylation via direct interaction with the substrate proteinN- and C-terminal domains in human holocarboxylase synthetase participate in substrate recognitionBiotin deficiency reduces expression of SLC19A3, a potential biotin transporter, in leukocytes from human blood.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 motifSolution structure of the LexA repressor DNA binding domain determined by 1H NMR spectroscopyLipoylating and biotinylating enzymes contain a homologous catalytic moduleA minimal peptide substrate in biotin holoenzyme synthetase-catalyzed biotinylationContinuous and discontinuous domains: an algorithm for the automatic generation of reliable protein domain definitionsProkaryotic 2-component systems and the OmpR/PhoB superfamilyThe three-dimensional structure of the RNA-binding domain of ribosomal protein L2; a protein at the peptidyl transferase center of the ribosomeStructure of the central core domain of TFIIEbeta with a novel double-stranded DNA-binding surfaceCorepressor-induced organization and assembly of the biotin repressor: A model for allosteric activation of a transcriptional regulatorAn Src homology 3-like domain is responsible for dimerization of the repressor protein KorB encoded by the promiscuous IncP plasmid RP4Determinants of the Src Homology Domain 3-Like FoldThe Purine Repressor of Bacillus subtilis: a Novel Combination of Domains Adapted for Transcription RegulationStructural analysis reveals DNA binding properties of Rv2827c, a hypothetical protein from Mycobacterium tuberculosisGlobal Conformational Change Associated with the Two-step Reaction Catalyzed by Escherichia coli Lipoate-Protein Ligase AStructural Ordering of Disordered Ligand-Binding Loops of Biotin Protein Ligase into Active Conformations as a Consequence of DehydrationActive site conformational changes upon reaction intermediate biotinyl-5'-AMP binding in biotin protein ligase fromMycobacterium tuberculosisCrystal structure of the SH3 domain in human Fyn; comparison of the three-dimensional structures of SH3 domains in tyrosine kinases and spectrinStructure of the multimodular endonuclease FokI bound to DNAStructural homology between the Rap30 DNA-binding domain and linker histone H5: implications for preinitiation complex assemblyBiotin protein ligase from Saccharomyces cerevisiae. The N-terminal domain is required for complete activity.Meet the neighbors: Mapping local protein interactomes by proximity-dependent labeling with BioIDThree-dimensional structure of the bifunctional protein PCD/DCoH, a cytoplasmic enzyme interacting with transcription factor HNF1The C-terminal domain of biotin protein ligase from E. coli is required for catalytic activityCompeting protein:protein interactions are proposed to control the biological switch of the E coli biotin repressorThe Mycobacterium tuberculosis LipB enzyme functions as a cysteine/lysine dyad acyltransferaseBrucella BioR regulator defines a complex regulatory mechanism for bacterial biotin metabolismInsights from the architecture of the bacterial transcription apparatusThermal unfolding of small proteins with SH3 domain folding pattern.Predicted structure of the extracellular region of ligand-gated ion-channel receptors shows SH2-like and SH3-like domains forming the ligand-binding siteStructural similarities in the noncatalytic domains of phenylalanyl-tRNA and biotin synthetasesOverview of protein structural and functional folds.Selection of an active enzyme by phage display on the basis of the enzyme's catalytic activity in vivo.Ligand specificity of group I biotin protein ligase of Mycobacterium tuberculosisAllosteric signaling in the biotin repressor occurs via local folding coupled to global dampening of protein dynamics.Lipoic acid metabolism in microbial pathogens.Oxaloacetate synthesis in the methanarchaeon Methanosarcina barkeri: pyruvate carboxylase genes and a putative Escherichia coli-type bifunctional biotin protein ligase gene (bpl/birA) exhibit a unique organization.
P2860
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P2860
Escherichia coli biotin holoenzyme synthetase/bio repressor crystal structure delineates the biotin- and DNA-binding domains
description
1992 nî lūn-bûn
@nan
1992 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1992 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
name
Escherichia coli biotin holoen ...... iotin- and DNA-binding domains
@ast
Escherichia coli biotin holoen ...... iotin- and DNA-binding domains
@en
Escherichia coli biotin holoen ...... iotin- and DNA-binding domains
@nl
type
label
Escherichia coli biotin holoen ...... iotin- and DNA-binding domains
@ast
Escherichia coli biotin holoen ...... iotin- and DNA-binding domains
@en
Escherichia coli biotin holoen ...... iotin- and DNA-binding domains
@nl
prefLabel
Escherichia coli biotin holoen ...... iotin- and DNA-binding domains
@ast
Escherichia coli biotin holoen ...... iotin- and DNA-binding domains
@en
Escherichia coli biotin holoen ...... iotin- and DNA-binding domains
@nl
P2093
P2860
P3181
P356
P1476
Escherichia coli biotin holoen ...... iotin- and DNA-binding domains
@en
P2093
A J Otsuka
B W Matthews
K P Wilson
L M Shewchuk
R G Brennan
P2860
P304
P3181
P356
10.1073/PNAS.89.19.9257
P407
P577
1992-10-01T00:00:00Z