The NMR structure of Escherichia coli ribosomal protein L25 shows homology to general stress proteins and glutaminyl-tRNA synthetases

EMBO Journal

Volumn 17, Issue 21, 1998, Pages 6377-6384

  Stoldt, Matthias ^a   Wöhnert, Jens ^a   Görlach, Matthias ^a   Brown, Larry R ^a  

^a FRITZ LIPMANN INSTITUTE   (Germany)

Author keywords

NMR spectroscopy; Protein structure; Ribosomal protein; Ribosome; RNA binding

Indexed keywords

CARBON 13; GLUTAMINE TRANSFER RNA LIGASE; HEAT SHOCK PROTEIN; NITROGEN 15; RIBOSOME PROTEIN; RNA 5S; RNA BINDING PROTEIN; TRANSFER RNA;

ALPHA HELIX; ANTICODON; ARTICLE; BETA CHAIN; ESCHERICHIA COLI; EUBACTERIUM; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN STRUCTURE; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; AMINO ACYL-TRNA SYNTHETASES; BACTERIAL PROTEINS; BINDING SITES; ESCHERICHIA COLI; HEAT-SHOCK PROTEINS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NUCLEIC ACID CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RIBOSOMAL PROTEINS; RNA, RIBOSOMAL, 5S; RNA-BINDING PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; NEGIBACTERIA;

EID: 0032476667     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/17.21.6377     Document Type: Article

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