Construction of heterodimer tyrosyl-tRNA synthetase shows tRNATyr interacts with both subunits
about
2.9 Å crystal structure of ligand-free tryptophanyl-tRNA synthetase: Domain movements fragment the adenine nucleotide binding siteEvolution of RNA-protein interactions: non-specific binding led to RNA splicing activity of fungal mitochondrial tyrosyl-tRNA synthetasesConserved amino acids near the carboxy terminus of bacterial tyrosyl-tRNA synthetase are involved in tRNA and Tyr-AMP binding.Detection of noncovalent tRNA.aminoacyl-tRNA synthetase complexes by matrix-assisted laser desorption/ionization mass spectrometry.Relaxed substrate specificity leads to extensive tRNA mischarging by Streptococcus pneumoniae class I and class II aminoacyl-tRNA synthetasesRemodeling domain interfaces to enhance heterodimer formationAn unusual RNA tertiary interaction has a role for the specific aminoacylation of a transfer RNA.Role of dimerization in yeast aspartyl-tRNA synthetase and importance of the class II invariant prolineDomain-domain communication in a miniature archaebacterial tRNA synthetase.Structural Divergence of the Group I Intron Binding Surface in Fungal Mitochondrial Tyrosyl-tRNA Synthetases That Function in RNA Splicing.Toward the catalytic mechanism of a cysteine ligase (MshC) from Mycobacterium smegmatis: an enzyme involved in the biosynthetic pathway of mycothiol.Sequence determination and modeling of structural motifs for the smallest monomeric aminoacyl-tRNA synthetase.Seryl-tRNA synthetase from Escherichia coli: functional evidence for cross-dimer tRNA binding during aminoacylation.Aminoacylation of RNA minihelices: implications for tRNA synthetase structural design and evolution.Protein engineering. The design, synthesis and characterization of factitious proteins.Dissociation of enzyme oligomers: a mechanism for allosteric regulation.Probing the molecular mechanisms in copper amine oxidases by generating heterodimers.Major anticodon-binding region missing from an archaebacterial tRNA synthetase.NMR Structure of the C-terminal domain of a tyrosyl-tRNA synthetase that functions in group I intron splicing
P2860
Q27621756-A0C8EF1D-1D05-4E87-9CB6-2C409A69CB1DQ28542826-A8847E1C-CC7E-4917-88E9-5008F511626DQ32148443-EA96F5FC-C420-4755-892C-61138401B05AQ32172085-6F850CB7-99EF-447C-818A-32E9C6FE18F3Q34237902-5ED476B4-2534-48F5-8507-A93F71BA65D4Q36282258-04369DF3-4DB8-4113-B2AF-D6B38F4BF67FQ36430629-A60FCCDA-F496-4767-AF25-E56CBF44983DQ36675264-4DD15148-8233-4C46-BC4E-EA1FB4EF619EQ36698512-56E2D03A-D482-48E7-B3C6-9AB8A970D522Q36941149-17C4DAB0-F073-4F93-816B-73633C149194Q37356885-4A76325F-1E92-4D73-967B-FCF041BF75B9Q37390421-A82337C8-6EA1-4FCC-A111-07C49581F94EQ38296669-11A63697-B92F-41C1-9493-738F52EE26C7Q38323262-5A4FD064-5B72-49B4-ACDF-B83819A096E8Q39677448-AF26CAB0-0076-4DF2-8AD3-01C4F0AF5D24Q40668995-C965B02D-AD14-4EA9-AF30-D80E5F71B433Q41170051-ECE08820-3C96-44EF-B1BA-2CD5CBAA43F7Q41705557-1A47CA7D-A762-4605-B813-46111BE77F49Q41820586-E356ED29-515D-4F05-B29B-5F2F7B7944AE
P2860
Construction of heterodimer tyrosyl-tRNA synthetase shows tRNATyr interacts with both subunits
description
1986 nî lūn-bûn
@nan
1986 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1986 թվականի մարտին հրատարակված գիտական հոդված
@hy
1986年の論文
@ja
1986年論文
@yue
1986年論文
@zh-hant
1986年論文
@zh-hk
1986年論文
@zh-mo
1986年論文
@zh-tw
1986年论文
@wuu
name
Construction of heterodimer ty ...... r interacts with both subunits
@ast
Construction of heterodimer ty ...... r interacts with both subunits
@en
Construction of heterodimer ty ...... r interacts with both subunits
@nl
type
label
Construction of heterodimer ty ...... r interacts with both subunits
@ast
Construction of heterodimer ty ...... r interacts with both subunits
@en
Construction of heterodimer ty ...... r interacts with both subunits
@nl
prefLabel
Construction of heterodimer ty ...... r interacts with both subunits
@ast
Construction of heterodimer ty ...... r interacts with both subunits
@en
Construction of heterodimer ty ...... r interacts with both subunits
@nl
P2093
P2860
P356
P1476
Construction of heterodimer ty ...... r interacts with both subunits
@en
P2093
P2860
P304
P356
10.1073/PNAS.83.5.1189
P407
P577
1986-03-01T00:00:00Z