The crystal structure of Cys-tRNACys-EF-Tu-GDPNP reveals general and specific features in the ternary complex and in tRNA
about
Elongation in translation as a dynamic interaction among the ribosome, tRNA, and elongation factors EF-G and EF-TuCrystal structure of the phosphorolytic exoribonuclease RNase PH from Bacillus subtilis and implications for its quaternary structure and tRNA bindingTools for the automatic identification and classification of RNA base pairsSubstrate discrimination in RNase P RNA-mediated cleavage: importance of the structural environment of the RNase P cleavage siteSolution structure of psi32-modified anticodon stem-loop of Escherichia coli tRNAPhe.A unique tRNA recognition mechanism of Caenorhabditis elegans mitochondrial EF-Tu2.Structure of transfer RNAs: similarity and variabilityStructures and functions of Qβ replicase: translation factors beyond protein synthesisStructure of the fMet-tRNAfMet-binding domain of B.stearothermophilus initiation factor IF2Conformational change of elongation factor Tu (EF-Tu) induced by antibiotic binding. Crystal structure of the complex between EF-Tu.GDP and aurodoxThe crystal structure of Sulfolobus solfataricus elongation factor 1alpha in complex with GDP reveals novel features in nucleotide binding and exchangeV-shaped structure of glutamyl-tRNA reductase, the first enzyme of tRNA-dependent tetrapyrrole biosynthesis.Structural insights into the first step of RNA-dependent cysteine biosynthesis in archaeaCrystal structure of human selenocysteine tRNANMR structure of a 4 x 4 nucleotide RNA internal loop from an R2 retrotransposon: Identification of a three purine-purine sheared pair motif and comparison to MC-SYM predictionsConformation Effects of Base Modification on the Anticodon Stem–Loop of Bacillus subtilis tRNATyrCrystal structure of Cex1p reveals the mechanism of tRNA trafficking between nucleus and cytoplasmMolecular basis for RNA polymerization by Qβ replicaseSolution Nuclear Magnetic Resonance Analyses of the Anticodon Arms of Proteinogenic and Nonproteinogenic tRNA Gly3DNA: a software package for the analysis, rebuilding and visualization of three-dimensional nucleic acid structuresKinetics of the interactions between yeast elongation factors 1A and 1Balpha, guanine nucleotides, and aminoacyl-tRNA.The Pseudomonas aeruginosa initiation factor IF-2 is responsible for formylation-independent protein initiation in P. aeruginosaCharacterization of mSelB, a novel mammalian elongation factor for selenoprotein translationThe mechanistic and evolutionary aspects of the 2'- and 3'-OH paradigm in biosynthetic machinerySelenocysteine tRNA-specific elongation factor SelB is a structural chimaera of elongation and initiation factorsStructure alignment-based classification of RNA-binding pockets reveals regional RNA recognition motifs on protein surfacesTandemly activated tRNAs as participants in protein synthesis.Multiple molecular dynamics simulation of the isoforms of human translation elongation factor 1A reveals reversible fluctuations between "open" and "closed" conformations and suggests specific for eEF1A1 affinity for Ca2+-calmodulinCrystal structures of the human elongation factor eEFSec suggest a non-canonical mechanism for selenocysteine incorporation.Novel thioredoxin targets in Dictyostelium discoideum identified by two-hybrid analysis: interactions of thioredoxin with elongation factor 1alpha and yeast alcohol dehydrogenase.A genetically encoded fluorescent tRNA is active in live-cell protein synthesis.A comprehensive, quantitative, and genome-wide model of translationStructural information for explaining the molecular mechanism of protein biosynthesis.Activation of initiation factor 2 by ligands and mutations for rapid docking of ribosomal subunitsAn ancient family of SelB elongation factor-like proteins with a broad but disjunct distribution across archaeaMacromolecular mimicryThe non-Watson-Crick base pairs and their associated isostericity matrices.GTPases mechanisms and functions of translation factors on the ribosome.The tRNA specificity of Thermus thermophilus EF-Tu.Eukaryotic initiator tRNA: finely tuned and ready for action.
P2860
Q24633187-BE0421A5-D9A1-45BA-B641-0DE18916921CQ24645212-77D715DE-916A-452A-A4B3-C07F0602A2E9Q24672574-D3D552D8-E390-4429-82A3-41A8FB415B97Q24791779-E6341AB7-70C7-4FB3-9148-E7E0C908F668Q24814281-45FD2C9C-7BE7-4944-B472-A95FE4707A44Q24814705-66011273-8470-4AF4-B426-28F5E9FF784BQ26824405-8D850444-9B16-49AB-8543-24A558AA9B5CQ27010178-54715EF2-736F-4B18-85B3-26FD1CB257C2Q27622305-B06D7C02-67AB-4A86-B297-58801700F248Q27630920-AB8474D6-3BA5-410A-BC1D-20B3252D68AFQ27635042-48D1FFED-2828-49F3-B79E-63C7D1CA3500Q27636477-22074EC5-E555-4D66-84DF-8A6916F58803Q27644031-31D5F41E-FE3B-4344-8F07-30FB4C39DFB5Q27657082-3311125B-C8EB-4CD5-B265-24ED13365125Q27670924-D82C166F-58D3-4EE8-83EB-B269C71301C1Q27670963-A1265129-9647-40E2-8166-B5A59ABDD88FQ27676291-561A2543-CF9E-469B-B5D6-BDBCF3CE487CQ27676753-87E57037-4172-4FEE-9232-1F04F801A7D5Q27678299-5F66EB76-1A8D-48A1-A73A-E1BFB3303E07Q27860547-852A6396-CB27-43D6-B5BB-23A17459DC62Q27937618-8C392A45-3F25-45E1-8AA8-45EBC69052AFQ28492995-89B44A7C-C928-427B-BEF5-1BDF6F2FD6F2Q28592967-A2E5EA8B-9B9E-4D41-A16E-8C24F3AF2297Q28676991-F54422BC-9BFD-4BCA-B1EF-1E8756B97468Q30160371-70047D2D-218D-41D3-9278-33BD27C3FA80Q30397328-4B7DF18E-FAA9-46E9-B685-D4C896BEA5A0Q30439843-87EB71BF-025B-4C90-AAE2-056852A8EBB9Q30481555-914CAE2E-8473-443A-B7B5-E3F0A5112D9EQ30821031-F6AE5F68-FCD3-4308-BF2E-8A672DCD1676Q31141673-86B7999C-8F55-4D9C-AE83-2A79A9040EB2Q33580457-6E51CD14-098E-4F61-8C04-4B5A6FABC06CQ33649778-4BB0C96B-5FD5-42E8-BE7A-2E049DC507F0Q33665572-03A102D7-377E-4BB7-BB46-CBC5DB058C50Q33768709-CD4D39DA-372D-484C-A2B6-80AB84352484Q33799965-2B53E3C5-9D9E-40D7-ACD9-B6A1702AA240Q33838081-A6ACB375-B388-4A2A-AD36-A64BDC8AEDF9Q33960863-03EC4765-BE68-499A-BCEA-9DCC514D2A0EQ33999568-8478F76E-28A5-4618-A666-0893C3137189Q34018710-8B6D4691-7763-4BB2-A4A5-7DD5411FF6C4Q34020233-54D664B9-0302-4DE8-ABF0-C0426828055A
P2860
The crystal structure of Cys-tRNACys-EF-Tu-GDPNP reveals general and specific features in the ternary complex and in tRNA
description
1999 nî lūn-bûn
@nan
1999 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի փետրվարին 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 crystal structure of Cys-t ...... he ternary complex and in tRNA
@ast
The crystal structure of Cys-t ...... he ternary complex and in tRNA
@en
The crystal structure of Cys-t ...... he ternary complex and in tRNA
@nl
type
label
The crystal structure of Cys-t ...... he ternary complex and in tRNA
@ast
The crystal structure of Cys-t ...... he ternary complex and in tRNA
@en
The crystal structure of Cys-t ...... he ternary complex and in tRNA
@nl
prefLabel
The crystal structure of Cys-t ...... he ternary complex and in tRNA
@ast
The crystal structure of Cys-t ...... he ternary complex and in tRNA
@en
The crystal structure of Cys-t ...... he ternary complex and in tRNA
@nl
P3181
P1433
P1476
The crystal structure of Cys-t ...... he ternary complex and in tRNA
@en
P2093
M Kjeldgaard
P304
P3181
P356
10.1016/S0969-2126(99)80021-5
P577
1999-02-15T00:00:00Z