Aspartyl tRNA-synthetase from Escherichia coli: Flexibility and adaptability to the substrates

Journal of Molecular Biology

Volumn 299, Issue 5, 2000, Pages 1157-1164

  Rees, Bernard ^a   Webster, Gordon ^a   Delarue, Marc ^a   Boeglin, Marcel ^a   Moras, Dino ^a  

^a INSTITUT DE GÉNÉTIQUE ET DE BIOLOGIE MOLÉCULAIRE ET CELLULAIRE   (France)

Author keywords

Aminoacylation; Aspartyl tRNA synthetase; Conformational changes; Crystal structure; Ligand binding

Indexed keywords

ASPARTATE TRANSFER RNA LIGASE; TRANSFER RNA;

AMINO TERMINAL SEQUENCE; AMINOACYLATION; ARTICLE; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; ENZYME STRUCTURE; ESCHERICHIA COLI; LIGAND BINDING; NONHUMAN; PRIORITY JOURNAL; PROTEIN INTERACTION; RNA BINDING; STRUCTURE ANALYSIS;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0034705343     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2000.3792     Document Type: Article

References (16)

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14. Class II aminoacyl transfer RNA synthetases: Crystal structure of yeast aspartyl-tRNA synthetase complexed with tRNA(Asp)
15. The free yeast aspartyl-tRNA synthetase differs from the tRNA(Asp)-complexed enzyme by structural changes in the catalytic site, hinge region, and anticodon binding domain
16. Crystal structure of aspartyl-tRNA synthetase from Pyrococcus kodakaraensis KOD: Archaeon specificity and catalytic mechanism of adenylate formation