Structure of pyrrolysyl-tRNA synthetase, an archaeal enzyme for genetic code innovation - Wikidata - wikimedia - TriplyDB

Structure of pyrrolysyl-tRNA synthetase, an archaeal enzyme for genetic code innovation

Structure of pyrrolysyl-tRNA synthetase, an archaeal enzyme for genetic code innovation

http://www.wikidata.org/entity/Q27646434

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Selenocysteine, pyrrolysine, and the unique energy metabolism of methanogenic archaea Carbon source-dependent expansion of the genetic code in bacteria A facile system for encoding unnatural amino acids in mammalian cells Pyrrolysyl-tRNA synthetase-tRNA(Pyl) structure reveals the molecular basis of orthogonality Pyrrolysyl-tRNA synthetase: an ordinary enzyme but an outstanding genetic code expansion tool Structure of Desulfitobacterium hafniense PylSc, a pyrrolysyl-tRNA synthetase Stereochemical Basis for Engineered Pyrrolysyl-tRNA Synthetase and the Efficient in Vivo Incorporation of Structurally Divergent Non-native Amino Acids Structural basis for the site-specific incorporation of lysine derivatives into proteins A 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 site Ancient translation factor is essential for tRNA-dependent cysteine biosynthesis in methanogenic archaea Structural insights into incorporation of norbornene amino acids for click modification of proteins Structural basis of furan-amino acid recognition by a polyspecific aminoacyl-tRNA-synthetase and its genetic encoding in human cells Ancient origin of the divergent forms of leucyl-tRNA synthetases in the Halobacteriales Bridging the gap between ribosomal and nonribosomal protein synthesis Prospects of In vivo Incorporation of Non-canonical Amino Acids for the Chemical Diversification of Antimicrobial Peptides Genetically encoded optochemical probes for simultaneous fluorescence reporting and light activation of protein function with two-photon excitation.Design of S-Allylcysteine in Situ Production and Incorporation Based on a Novel Pyrrolysyl-tRNA Synthetase Variant.Expanding the genetic code of mammalian cells.Introduction of a leucine half-zipper engenders multiple high-quality crystals of a recalcitrant tRNA synthetase From one amino acid to another: tRNA-dependent amino acid biosynthesis Exploring the substrate range of wild-type aminoacyl-tRNA synthetases.Pathways of Genetic Code Evolution in Ancient and Modern Organisms.Polyspecific pyrrolysyl-tRNA synthetases from directed evolution Adding pyrrolysine to the Escherichia coli genetic code.Expanding the library and substrate diversity of the pyrrolysyl-tRNA synthetase to incorporate unnatural amino acids containing conjugated rings.Functional context, biosynthesis, and genetic encoding of pyrrolysine.Synthesis of non-linear protein dimers through a genetically encoded Thiol-ene reaction.Ancient horizontal gene transfer and the last common ancestors A rationally designed pyrrolysyl-tRNA synthetase mutant with a broad substrate spectrum Catalyst-free and site-specific one-pot dual-labeling of a protein directed by two genetically incorporated noncanonical amino acids Genetically encoded fluorophenylalanines enable insights into the recognition of lysine trimethylation by an epigenetic reader.PylSn and the homologous N-terminal domain of pyrrolysyl-tRNA synthetase bind the tRNA that is essential for the genetic encoding of pyrrolysine Probing the active site tryptophan of Staphylococcus aureus thioredoxin with an analog.N6-(2-(R)-propargylglycyl)lysine as a clickable pyrrolysine mimic.Genetic code flexibility in microorganisms: novel mechanisms and impact on physiology.Genetic incorporation of twelve meta-substituted phenylalanine derivatives using a single pyrrolysyl-tRNA synthetase mutant Efficient Reassignment of a Frequent Serine Codon in Wild-Type Escherichia coli.The homotetrameric phosphoseryl-tRNA synthetase from Methanosarcina mazei exhibits half-of-the-sites activity.Amino acid modifications on tRNA.Misacylation of pyrrolysine tRNA in vitro and in vivo.

P2860

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P2860

Structure of pyrrolysyl-tRNA synthetase, an archaeal enzyme for genetic code innovation

http://www.wikidata.org/entity/Q27646434

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2007 nî lūn-bûn

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2007 թուականի Յուլիսին հրատարակուած գիտական յօդուած

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2007年の論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年论文

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Structure of pyrrolysyl-tRNA synthetase, an archaeal enzyme for genetic code innovation

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Structure of pyrrolysyl-tRNA synthetase, an archaeal enzyme for genetic code innovation

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Structure of pyrrolysyl-tRNA synthetase, an archaeal enzyme for genetic code innovation

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Structure of pyrrolysyl-tRNA synthetase, an archaeal enzyme for genetic code innovation

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Structure of pyrrolysyl-tRNA synthetase, an archaeal enzyme for genetic code innovation

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Structure of pyrrolysyl-tRNA synthetase, an archaeal enzyme for genetic code innovation

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Structure of pyrrolysyl-tRNA synthetase, an archaeal enzyme for genetic code innovation

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Structure of pyrrolysyl-tRNA synthetase, an archaeal enzyme for genetic code innovation

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Structure of pyrrolysyl-tRNA synthetase, an archaeal enzyme for genetic code innovation

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

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Structure of pyrrolysyl-tRNA synthetase, an archaeal enzyme for genetic code innovation

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Jennifer M Kavran

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Markus Englert

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Patrick O'Donoghue

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Sarath Gundllapalli

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Thomas A Steitz

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P2860

The Protein Data Bank

On the evolution of cells

Aminoacyl-tRNA synthetases, the genetic code, and the evolutionary process

An aminoacyl-tRNA synthetase that specifically activates pyrrolysine

On the evolution of structure in aminoacyl-tRNA synthetases

Emergence of the universal genetic code imprinted in an RNA record

Pyrrolysine is not hardwired for cotranslational insertion at UAG codons

The integrated microbial genomes (IMG) system

Active site of lysyl-tRNA synthetase: structural studies of the adenylation reaction

Structure at 2.6 A resolution of phenylalanyl-tRNA synthetase complexed with phenylalanyl-adenylate in the presence of manganese

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104

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