The first step of aminoacylation at the atomic level in histidyl-tRNA synthetase - Test2 - elhamkhani - TriplyDB

The first step of aminoacylation at the atomic level in histidyl-tRNA synthetase

The first step of aminoacylation at the atomic level in histidyl-tRNA synthetase

http://www.wikidata.org/entity/Q27740004

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Characterization of a mammalian homolog of the GCN2 eukaryotic initiation factor 2alpha kinase Mutations in mitochondrial histidyl tRNA synthetase HARS2 cause ovarian dysgenesis and sensorineural hearing loss of Perrault syndrome Crystal structure of aspartyl-tRNA synthetase from Pyrococcus kodakaraensis KOD: archaeon specificity and catalytic mechanism of adenylate formation.An aminoacyl-tRNA synthetase paralog with a catalytic role in histidine biosynthesis Functional Class I and II Amino Acid-activating Enzymes Can Be Coded by Opposite Strands of the Same Gene Substrate induced conformational changes in argininosuccinate synthetase Crystal Structure of Tryptophanyl-tRNA Synthetase Complexed with Adenosine-5′ Tetraphosphate: Evidence for Distributed Use of Catalytic Binding Energy in Amino Acid Activation by Class I Aminoacyl-tRNA Synthetases Crystal Structures of Trypanosomal Histidyl-tRNA Synthetase Illuminate Differences between Eukaryotic and Prokaryotic Homologs Histidyl-tRNA synthetase The mechanistic and evolutionary aspects of the 2'- and 3'-OH paradigm in biosynthetic machinery Identification of lethal mutations in yeast threonyl-tRNA synthetase revealing critical residues in its human homolog.Breaking sieve for steric exclusion of a noncognate amino acid from active site of a tRNA synthetase.Comparison of histidine recognition in human and trypanosomatid histidyl-tRNA synthetases.Biosynthesis of Histidine.Histidyl-tRNA synthetase urzymes: Class I and II aminoacyl tRNA synthetase urzymes have comparable catalytic activities for cognate amino acid activation.Interaction between the tRNA-binding and C-terminal domains of Yeast Gcn2 regulates kinase activity in vivo.A binding hotspot in Trypanosoma cruzi histidyl-tRNA synthetase revealed by fragment-based crystallographic cocktail screens.Catalytic mechanism and allosteric regulation of an oligomeric (p)ppGpp synthetase by an alarmone.A genomically modified Escherichia coli strain carrying an orthogonal E. coli histidyl-tRNA synthetase•tRNAHis pair.DNA polymerases and aminoacyl-tRNA synthetases: shared mechanisms for ensuring the fidelity of gene expression Asymmetric amino acid activation by class II histidyl-tRNA synthetase from Escherichia coli.Toward the catalytic mechanism of a cysteine ligase (MshC) from Mycobacterium smegmatis: an enzyme involved in the biosynthetic pathway of mycothiol.Emergence and evolution.OB or Not OB: Idiosyncratic utilization of the tRNA-binding OB-fold domain in unicellular, pathogenic eukaryotes.cpc-3, the Neurospora crassa homologue of yeast GCN2, encodes a polypeptide with juxtaposed eIF2alpha kinase and histidyl-tRNA synthetase-related domains required for general amino acid control.Effect of G-1 on histidine tRNA microhelix conformation.Kinetic discrimination of tRNA identity by the conserved motif 2 loop of a class II aminoacyl-tRNA synthetase.The α-amino group of the threonine substrate as the general base during tRNA aminoacylation: a new version of substrate-assisted catalysis predicted by hybrid DFT.The crystal structure of asparaginyl-tRNA synthetase from Thermus thermophilus and its complexes with ATP and asparaginyl-adenylate: the mechanism of discrimination between asparagine and aspartic acid.Aminoacylation at the Atomic Level in Class IIa Aminoacyl-tRNA Synthetases.Activation of the hetero-octameric ATP phosphoribosyl transferase through subunit interface rearrangement by a tRNA synthetase paralog.Dynamics of the active site loops in catalyzing aminoacylation reaction in seryl and histidyl tRNA synthetases.Mechanism of the activation step of the aminoacylation reaction: a significant difference between class I and class II synthetases.

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The first step of aminoacylation at the atomic level in histidyl-tRNA synthetase

http://www.wikidata.org/entity/Q27740004

description

1997 nî lūn-bûn

@nan

1997 թուականի Յուլիսին հրատարակուած գիտական յօդուած

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1997 թվականի հուլիսին հրատարակված գիտական հոդված

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1997年の論文

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1997年論文

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1997年論文

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1997年論文

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1997年論文

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1997年論文

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1997年论文

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name

The first step of aminoacylation at the atomic level in histidyl-tRNA synthetase

@ast

The first step of aminoacylation at the atomic level in histidyl-tRNA synthetase

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The first step of aminoacylation at the atomic level in histidyl-tRNA synthetase

@nl

type

label

The first step of aminoacylation at the atomic level in histidyl-tRNA synthetase

@ast

The first step of aminoacylation at the atomic level in histidyl-tRNA synthetase

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The first step of aminoacylation at the atomic level in histidyl-tRNA synthetase

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prefLabel

The first step of aminoacylation at the atomic level in histidyl-tRNA synthetase

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The first step of aminoacylation at the atomic level in histidyl-tRNA synthetase

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The first step of aminoacylation at the atomic level in histidyl-tRNA synthetase

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Proceedings of the National Academy of Sciences of the United States of America

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The first step of aminoacylation at the atomic level in histidyl-tRNA synthetase

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C S Francklyn

http://www.w3.org/2001/XMLSchema#string

D Moras

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J G Arnez

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J G Augustine

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P2860

Enzyme-Catalyzed Phosphoryl Transfer Reactions

A general two-metal-ion mechanism for catalytic RNA

Improved methods for building protein models in electron density maps and the location of errors in these models

PROCHECK: a program to check the stereochemical quality of protein structures

MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

Reaction mechanism of alkaline phosphatase based on crystal structures. Two-metal ion catalysis

Structure of E. coli glutaminyl-tRNA synthetase complexed with tRNA(Gln) and ATP at 2.8 A resolution

Structure of tyrosyl-tRNA synthetase refined at 2.3 A resolution. Interaction of the enzyme with the tyrosyl adenylate intermediate

Crystal structure of histidyl-tRNA synthetase from Escherichia coli complexed with histidyl-adenylate

The crystal structure of the lysyl-tRNA synthetase (LysU) from Escherichia coli

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