The structure of threonyl-tRNA synthetase-tRNA(Thr) complex enlightens its repressor activity and reveals an essential zinc ion in the active site
about
Crystal structure of human wildtype and S581L-mutant glycyl-tRNA synthetase, an enzyme underlying distal spinal muscular atrophyCrystal structures and biochemical analyses suggest a unique mechanism and role for human glycyl-tRNA synthetase in Ap4A homeostasisPost-transfer editing in vitro and in vivo by the beta subunit of phenylalanyl-tRNA synthetasePyrrolysyl-tRNA synthetase-tRNA(Pyl) structure reveals the molecular basis of orthogonalityTools for the automatic identification and classification of RNA base pairsCrystal structure of the YchF protein reveals binding sites for GTP and nucleic acidStructure of Hsp15 reveals a novel RNA-binding motifCrystal structure of YbaK protein from Haemophilus influenzae (HI1434) at 1.8 A resolution: functional implicationsFunctional implications from crystal structures of the conserved Bacillus subtilis protein Maf with and without dUTPtRNA aminoacylation by arginyl-tRNA synthetase: induced conformations during substrates bindingCrystal structure of the quorum-sensing protein LuxS reveals a catalytic metal siteStructural and mutational studies of the recognition of the arginine tRNA-specific major identity element, A20, by arginyl-tRNA synthetaseRibosome-associated factor Y adopts a fold resembling a double-stranded RNA binding domain scaffoldCrystal structure of tRNA(m1G37)methyltransferase: insights into tRNA recognitionThe Solution Structure of YbcJ from Escherichia coli Reveals a Recently Discovered L Motif Involved in RNA BindingDNA mimicry by a high-affinity anti-NF- B RNA aptamerThe 1.6 Å Crystal Structure of Mycobacterium smegmatis MshC: The Penultimate Enzyme in the Mycothiol Biosynthetic Pathway †Unique protein architecture of alanyl-tRNA synthetase for aminoacylation, editing, and dimerizationThe C-Ala Domain Brings Together Editing and Aminoacylation Functions on One tRNACrystal Structures of Trypanosomal Histidyl-tRNA Synthetase Illuminate Differences between Eukaryotic and Prokaryotic HomologsATP-directed capture of bioactive herbal-based medicine on human tRNA synthetaseYeast mitochondrial threonyl-tRNA synthetase recognizes tRNA isoacceptors by distinct mechanisms and promotes CUN codon reassignmentCocrystal Structures of Glycyl-tRNA Synthetase in Complex with tRNA Suggest Multiple Conformational States in GlycylationThe selective tRNA aminoacylation mechanism based on a single G•U pairA missense mutation in the nuclear gene coding for the mitochondrial aspartyl-tRNA synthetase suppresses a mitochondrial tRNA(Asp) mutationTrans-editing of mischarged tRNAs.Pre-transfer editing by class II prolyl-tRNA synthetase: role of aminoacylation active site in "selective release" of noncognate amino acids.A Human Disease-causing Point Mutation in Mitochondrial Threonyl-tRNA Synthetase Induces Both Structural and Functional DefectsAcyl carrier protein/SpoT interaction, the switch linking SpoT-dependent stress response to fatty acid metabolismtRNA as an active chemical scaffold for diverse chemical transformationsRNA-assisted catalysis in a protein enzyme: The 2'-hydroxyl of tRNA(Thr) A76 promotes aminoacylation by threonyl-tRNA synthetaseIdentification of lethal mutations in yeast threonyl-tRNA synthetase revealing critical residues in its human homolog.Comparative metaproteomic analysis on consecutively Rehmannia glutinosa-monocultured rhizosphere soil.Structural basis for full-spectrum inhibition of translational functions on a tRNA synthetaseAminoacyl-Transfer RNA Synthetase Deficiency Promotes Angiogenesis via the Unfolded Protein Response PathwayThe prokaryotic antecedents of the ubiquitin-signaling system and the early evolution of ubiquitin-like beta-grasp domains.Discrimination between distant homologs and structural analogs: lessons from manually constructed, reliable data setsConformational changes in human prolyl-tRNA synthetase upon binding of the substrates proline and ATP and the inhibitor halofuginone.Small but versatile: the extraordinary functional and structural diversity of the beta-grasp foldPre-mRNA secondary structures influence exon recognition.
P2860
Q24307723-7AC960B7-0CE5-44CD-AB49-295295C5F58CQ24310019-52545426-F3D0-4AFB-8DF2-60A935F3CDB9Q24559890-3A0C8448-D61D-4538-925E-BB9DFFC5F4D3Q24647392-0384DC34-AB47-41B7-9408-7CFC61E9AF00Q24672574-70DE9203-0159-4B1A-9C78-4C461C02B565Q24682960-2695F1B7-55A4-44EF-BF9B-21F54D724B35Q27621387-4A611368-3281-4054-8C55-F443ED3F6483Q27622559-BB13A260-B866-4CC0-800C-2CCF6B9CFD74Q27622733-5CA677B8-05CC-4155-A82C-2C2F65CB8AB0Q27627790-81433598-9B3F-4761-BC76-901B1F21B375Q27634804-0A491834-7DFD-4353-97A0-AFE088537662Q27636050-5AFCDAF7-53DA-403C-A50F-FEA8CBD43076Q27639870-BC58F3B2-F968-4AD8-B340-BF7BB5BB54F1Q27641339-982AEF27-07D3-4913-8EE1-AB3C669BC3CCQ27641596-2A4D4C56-EE77-4C50-AEED-CCC2FCB73C4EQ27649437-BB75E205-1CA9-4386-8A35-E3531D0F0535Q27653039-2514CEE7-1335-4347-935C-7DB3A6754C81Q27655412-EF4414C4-5524-451F-8F64-5CC039117A6FQ27656913-F5255D30-6962-4F77-A7B1-371112E0D1C4Q27659528-30FB67EB-FFA0-44DD-85B2-8FD9C993D84BQ27675589-695A88AF-2E9C-4379-A38E-4A564BCF3344Q27677330-0EA3401A-D5E3-4BA5-84B0-9A7CDC698E68Q27684083-4F007174-4EAF-4692-BEC9-92AF306A0881Q27684299-F0721090-6A36-4E1E-9810-AF759BA3C239Q27932505-BF435DB2-D5AA-4AC8-B3EA-CFD9A5C9CCCFQ27938898-D064746C-495F-4C3F-B5E1-C8C5A596E970Q27939503-095DDBBA-3AC4-423C-8774-713F64F58A42Q28115437-12CFC67C-9260-4ECF-BE79-7D4AE37FCF8FQ28271588-F8264EBD-4CE6-445B-9D7B-BF21A2FA8D1CQ28741217-37BF4008-9F09-418C-834A-B63FBDA5043EQ28756526-3A9DDF99-6842-421B-BF8C-100985A4AE62Q30368860-F8486E41-338F-4B74-9025-E7C89AEEE162Q30396171-073B7DD0-B370-46A5-A6AA-375598F978A4Q30636920-1EE2AC2C-3D94-4149-9872-DFF3DE18CE71Q30733232-E0D5A552-6A13-4AB0-98DF-AE4DEBC00496Q30820062-F38DD575-D219-4BD7-B154-D8A43241655EQ31148267-96772616-2788-4356-8023-564E9AB872D2Q32884591-220EAB84-9990-453F-9E03-783158129DA8Q33289671-0AA9E11A-6F6F-485E-A317-CB8246A6C682Q33306112-ED9E695E-43A1-4D71-95E9-62D37AFBF18E
P2860
The structure of threonyl-tRNA synthetase-tRNA(Thr) complex enlightens its repressor activity and reveals an essential zinc ion in the active site
description
1999 nî lūn-bûn
@nan
1999 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
The structure of threonyl-tRNA ...... al zinc ion in the active site
@ast
The structure of threonyl-tRNA ...... al zinc ion in the active site
@en
The structure of threonyl-tRNA ...... al zinc ion in the active site
@nl
type
label
The structure of threonyl-tRNA ...... al zinc ion in the active site
@ast
The structure of threonyl-tRNA ...... al zinc ion in the active site
@en
The structure of threonyl-tRNA ...... al zinc ion in the active site
@nl
prefLabel
The structure of threonyl-tRNA ...... al zinc ion in the active site
@ast
The structure of threonyl-tRNA ...... al zinc ion in the active site
@en
The structure of threonyl-tRNA ...... al zinc ion in the active site
@nl
P2093
P3181
P1433
P1476
The structure of threonyl-tRNA ...... al zinc ion in the active site
@en
P2093
A C Dock-Bregeon
B Ehresmann
C Ehresmann
M Springer
R Sankaranarayanan
P304
P3181
P356
10.1016/S0092-8674(00)80746-1
P407
P577
1999-04-30T00:00:00Z