A paralog of lysyl-tRNA synthetase aminoacylates a conserved lysine residue in translation elongation factor P

Nature Structural and Molecular Biology

Volumn 17, Issue 9, 2010, Pages 1136-1143

  Yanagisawa, Tatsuo ^a   Sumida, Tomomi ^a   Ishii, Ryohei ^a,b,c   Takemoto, Chie ^a   Yokoyama, Shigeyuki ^a,b  

^a RIKEN   (Japan)

^b UNIVERSITY OF TOKYO   (Japan)

^c WEILL CORNELL MEDICAL COLLEGE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ELONGATION FACTOR; ELONGATION FACTOR P; GENX ENZYME; LYSINE; LYSINE TRANSFER RNA LIGASE; POXA ENZYME; UNCLASSIFIED DRUG; YJEA ENZYME; YJEK ENZYME; FACTOR EF-P; PROTEIN BINDING;

ARTICLE; CRYSTAL STRUCTURE; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; PROTEIN INTERACTION; X RAY CRYSTALLOGRAPHY; AMINOACYLATION; ANIMAL; CHEMICAL STRUCTURE; CHEMISTRY; ENZYMOLOGY; GENETICS; HUMAN; METABOLISM; MUTATION; PHYLOGENY; PROTEIN PROCESSING; PROTEIN QUATERNARY STRUCTURE; PROTEIN TERTIARY STRUCTURE;

AMINOACYLATION; ANIMALS; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; HUMANS; LYSINE; LYSINE-TRNA LIGASE; MODELS, MOLECULAR; MUTATION; PEPTIDE ELONGATION FACTORS; PHYLOGENY; PROTEIN BINDING; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY;

ESCHERICHIA COLI;

EID: 77956339569     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.1889     Document Type: Article

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