Crystallographic study at 2.5 A resolution of the interaction of methionyl-tRNA synthetase from Escherichia coli with ATP.
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L-arginine recognition by yeast arginyl-tRNA synthetase.Human cytoplasmic isoleucyl-tRNA synthetase: selective divergence of the anticodon-binding domain and acquisition of a new structural unitA component of the multisynthetase complex is a multifunctional aminoacyl-tRNA synthetaseSequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetasesCrystal structure of histidyl-tRNA synthetase from Escherichia coli complexed with histidyl-adenylateCrystal structure of glycyl-tRNA synthetase from Thermus thermophilusThe active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation reactionThe first step of aminoacylation at the atomic level in histidyl-tRNA synthetaseHuman tyrosyl-tRNA synthetase shares amino acid sequence homology with a putative cytokinePurification and characterization of phosphopantetheine adenylyltransferase from Escherichia coliComparison of the catalytic roles played by the KMSKS motif in the human and Bacillus stearothermophilus trosyl-tRNA synthetasesAdenosine conformations of nucleotides bound to methionyl tRNA synthetase by transferred nuclear Overhauser effect spectroscopy.In vivo selection of lethal mutations reveals two functional domains in arginyl-tRNA synthetase.Transition state stabilization by the 'high' motif of class I aminoacyl-tRNA synthetases: the case of Escherichia coli methionyl-tRNA synthetase.Functional communication in the recognition of tRNA by Escherichia coli glutaminyl-tRNA synthetase.Small RNA helices as substrates for aminoacylation and their relationship to charging of transfer RNAs.Editing of errors in selection of amino acids for protein synthesisMethionyl-tRNA synthetase from Bacillus stearothermophilus: structural and functional identities with the Escherichia coli enzyme.Single sequence of a helix-loop peptide confers functional anticodon recognition on two tRNA synthetases.Possible role of aminoacyl-RNA complexes in noncoded peptide synthesis and origin of coded synthesis.Cloning and nucleotide sequence of the leucyl-tRNA synthetase gene of Bacillus subtilis.Acceptor end binding domain interactions ensure correct aminoacylation of transfer RNA.Metal-binding site in a class I tRNA synthetase localized to a cysteine cluster inserted into nucleotide-binding fold.Amino acid binding by the class I aminoacyl-tRNA synthetases: role for a conserved proline in the signature sequence.Idiographic representation of conserved domain of a class II tRNA synthetase of unknown structureDominant lethality by expression of a catalytically inactive class I tRNA synthetaseActivation of microhelix charging by localized helix destabilizationAn operational RNA code for amino acids and possible relationship to genetic codeDiversified sequences of peptide epitope for same-RNA recognition.The relationship between synthetic and editing functions of the active site of an aminoacyl-tRNA synthetaseEnzymatic aminoacylation of sequence-specific RNA minihelices and hybrid duplexes with methionine.Functional assembly of a randomly cleaved proteinCovalent methionylation of Escherichia coli methionyl-tRNA synthethase: identification of the labeled amino acid residues by matrix-assisted laser desorption-ionization mass spectrometryDominant negative inhibition by fragments of a monomeric enzyme.RNA binding determinant in some class I tRNA synthetases identified by alignment-guided mutagenesis.Structural similarities in glutaminyl- and methionyl-tRNA synthetases suggest a common overall orientation of tRNA bindingAminoacylation of RNA minihelices: implications for tRNA synthetase structural design and evolution.Cloning and sequence determination of the valS gene, encoding valyl-tRNA synthetase in Lactobacillus casei.Molecular cloning, sequence, structural analysis and expression of the histidyl-tRNA synthetase gene from Streptococcus equisimilis.A comparison of several similarity indices used in the classification of protein sequences: a multivariate analysis
P2860
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P2860
Crystallographic study at 2.5 A resolution of the interaction of methionyl-tRNA synthetase from Escherichia coli with ATP.
description
1990 nî lūn-bûn
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1990年の論文
@ja
1990年学术文章
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1990年学术文章
@zh-cn
1990年学术文章
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1990年学术文章
@zh-my
1990年学术文章
@zh-sg
1990年學術文章
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1990年學術文章
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1990年學術文章
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name
Crystallographic study at 2.5 ...... rom Escherichia coli with ATP.
@en
Crystallographic study at 2.5 ...... rom Escherichia coli with ATP.
@nl
type
label
Crystallographic study at 2.5 ...... rom Escherichia coli with ATP.
@en
Crystallographic study at 2.5 ...... rom Escherichia coli with ATP.
@nl
prefLabel
Crystallographic study at 2.5 ...... rom Escherichia coli with ATP.
@en
Crystallographic study at 2.5 ...... rom Escherichia coli with ATP.
@nl
P2093
P1476
Crystallographic study at 2.5 ...... rom Escherichia coli with ATP.
@en
P2093
P304
P356
10.1016/S0022-2836(05)80331-6
P407
P577
1990-11-01T00:00:00Z