Structural studies of lysyl-tRNA synthetase: conformational changes induced by substrate binding
about
Prokaryotic homologs of the eukaryotic DNA-end-binding protein Ku, novel domains in the Ku protein and prediction of a prokaryotic double-strand break repair systemFunctional asymmetry in the lysyl-tRNA synthetase explored by molecular dynamics, free energy calculations and experimentNon-discriminating and discriminating aspartyl-tRNA synthetases differ in the anticodon-binding domainCatalytic mechanism of the tryptophan activation reaction revealed by crystal structures of human tryptophanyl-tRNA synthetase in different enzymatic statesCrystal structure of tetrameric form of human lysyl-tRNA synthetase: Implications for multisynthetase complex formationA novel crystal form of pyrrolysyl-tRNA synthetase reveals the pre- and post-aminoacyl-tRNA synthesis conformational states of the adenylate and aminoacyl moieties and an asparagine residue in the catalytic siteCrystal structures of Entamoeba histolytica lysyl-tRNA synthetase reveal conformational changes upon lysine binding and a specific helix bundle domainProtein solubility and folding enhancement by interaction with RNAPredicting the pathway involved in post-translational modification of elongation factor P in a subset of bacterial species.Ligand co-crystallization of aminoacyl-tRNA synthetases from infectious disease organismsRational design of an orthogonal tryptophanyl nonsense suppressor tRNAAminoacyl-tRNA synthetases: versatile players in the changing theater of translation.Mechanisms of resistance to an amino acid antibiotic that targets translation.Discrimination of cognate and noncognate substrates at the active site of class I lysyl-tRNA synthetase.Emergence and evolution.The N-terminal domain of mammalian Lysyl-tRNA synthetase is a functional tRNA-binding domain.BOF: a novel family of bacterial OB-fold proteins.A bacterial ortholog of class II lysyl-tRNA synthetase activates lysine.Target specificity of an autoreactive pathogenic human γδ-T cell receptor in myositis.N-terminal domains of native multidomain proteins have the potential to assist de novo folding of their downstream domains in vivo by acting as solubility enhancersDivergence in noncognate amino acid recognition between class I and class II lysyl-tRNA synthetases.Transition state stabilization by the N-terminal anticodon-binding domain of lysyl-tRNA synthetase.Multiple catalytic activities of Escherichia coli lysyl-tRNA synthetase (LysU) are dissected by site-directed mutagenesis.Functional dissection of the eukaryotic-specific tRNA-interacting factor of lysyl-tRNA synthetase.Ammonium scanning in an enzyme active site. The chiral specificity of aspartyl-tRNA synthetase.5 S rRNA and tRNA import into human mitochondria. Comparison of in vitro requirements
P2860
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P2860
Structural studies of lysyl-tRNA synthetase: conformational changes induced by substrate binding
description
2000 nî lūn-bûn
@nan
2000 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Structural studies of lysyl-tR ...... s induced by substrate binding
@ast
Structural studies of lysyl-tR ...... s induced by substrate binding
@en
Structural studies of lysyl-tR ...... s induced by substrate binding
@nl
type
label
Structural studies of lysyl-tR ...... s induced by substrate binding
@ast
Structural studies of lysyl-tR ...... s induced by substrate binding
@en
Structural studies of lysyl-tR ...... s induced by substrate binding
@nl
prefLabel
Structural studies of lysyl-tR ...... s induced by substrate binding
@ast
Structural studies of lysyl-tR ...... s induced by substrate binding
@en
Structural studies of lysyl-tR ...... s induced by substrate binding
@nl
P2093
P356
P1433
P1476
Structural studies of lysyl-tR ...... s induced by substrate binding
@en
P2093
P304
P356
10.1021/BI001487R
P407
P577
2000-10-24T00:00:00Z