Literature DB >> 8199247

Yeast aspartyl-tRNA synthetase: a structural view of the aminoacylation reaction.

J Cavarelli1, B Rees, J C Thierry, D Moras.   

Abstract

The refinement of the crystal structure of a binary complex formed by yeast AspRS and tRNA(Asp) provided a detailed understanding of the recognition of tRNA by an aminoacyl-tRNA synthetase. The crystal structures of several complexes containing ATP, alone or with aspartic acid, were also determined and refined. These studies led to a complete description of the active site of the enzyme and to the elucidation of the location and interactions of the various substrates. Based on these structural results, a class II-specific pathway for the aminoacylation reaction can be proposed.

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Year:  1993        PMID: 8199247     DOI: 10.1016/0300-9084(93)90011-g

Source DB:  PubMed          Journal:  Biochimie        ISSN: 0300-9084            Impact factor:   4.079


  3 in total

1.  Footprinting of tRNA(Phe) transcripts from Thermus thermophilus HB8 with the homologous phenylalanyl-tRNA synthetase reveals a novel mode of interaction.

Authors:  R Kreutzer; D Kern; R Giegé; J Rudinger
Journal:  Nucleic Acids Res       Date:  1995-11-25       Impact factor: 16.971

2.  The discriminator bases G73 in human tRNA(Ser) and A73 in tRNA(Leu) have significantly different roles in the recognition of aminoacyl-tRNA synthetases.

Authors:  K Breitschopf; H J Gross
Journal:  Nucleic Acids Res       Date:  1996-02-01       Impact factor: 16.971

3.  Palindromes in proteins.

Authors:  Malgorzata Giel-Pietraszuk; Marcin Hoffmann; Sylwia Dolecka; Jacek Rychlewski; Jan Barciszewski
Journal:  J Protein Chem       Date:  2003-02
  3 in total

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