The crystal structure of asparaginyl-tRNA synthetase from Thermus thermophilus and its complexes with ATP and asparaginyl-adenylate: The mechanism of discrimination between asparagine and aspartic acid

EMBO Journal

Volumn 17, Issue 10, 1998, Pages 2947-2960

  Berthet Colominas, Carmen ^a   Seignovert, Laurence ^a   Härtlein, Michael ^a   Grotli, Morten ^b,c   Cusack, Stephen ^a   Leberman, Reuben ^a  

^a EUROPEAN MOLECULAR BIOLOGY LABORATORY   (France)

^b EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

^c CARLSBERG LABORATORY   (Denmark)

Author keywords

Aminoacyl tRNA synthetase; Asparagine; ATP; Enzyme specificity; X ray crystallography

Indexed keywords

ADENOSINE PHOSPHATE; ADENOSINE TRIPHOSPHATE; AMINO ACID TRANSFER RNA LIGASE; ASPARAGINE; ASPARAGINE TRANSFER RNA; ASPARTATE TRANSFER RNA LIGASE; ASPARTIC ACID; BACTERIAL ENZYME;

AMINO ACID SEQUENCE; ARTICLE; COMPLEX FORMATION; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME SPECIFICITY; ENZYME STRUCTURE; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN TERTIARY STRUCTURE; SEQUENCE HOMOLOGY; THERMUS THERMOPHILUS;

ADENOSINE TRIPHOSPHATE; AMINO ACID SEQUENCE; AMINO ACYL-TRNA SYNTHETASES; ASPARAGINE; ASPARTATE-TRNA LIGASE; ASPARTIC ACID; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; RNA, TRANSFER, AMINO ACYL; SEQUENCE HOMOLOGY, AMINO ACID; THERMUS THERMOPHILUS;

EID: 0032525301     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/17.10.2947     Document Type: Article

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