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Unique Protein Architecture of Alanyl-tRNA Synthetase for Aminoacylation, Editing, and Dimerization

Naganuma, Masahiro ; Sekine, Shun-Ichi ; Fukunaga, Ryuya ; Yokoyama, Shigeyuki ; Schimmel, Paul R.

Proceedings of the National Academy of Sciences of the United States of America, 26 May 2009, Vol.106(21), pp.8489-8494 [Rivista Peer Reviewed]

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  • Titolo:
    Unique Protein Architecture of Alanyl-tRNA Synthetase for Aminoacylation, Editing, and Dimerization
  • Autore: Naganuma, Masahiro ; Sekine, Shun-Ichi ; Fukunaga, Ryuya ; Yokoyama, Shigeyuki ; Schimmel, Paul R.
  • Descrizione: Alanyl-tRNA synthetase (AlaRS) specifically recognizes the major identity determinant, the G3:U7O base pair, in the acceptor stem of tRNA Ala by both the tRNA-recognition and editing domains. In this study, we solved the crystal structures of 2 halves of Archaeoglobus fulgidus AlaRS: AlaRS-ΔC, comprising the aminoacylation, tRNA-recognition, and editing domains, and AlaRS-C, comprising the dimerization domain. The aminoacylation/tRNA-recognition domains contain an insertion incompatible with the class-specific tRNA-binding mode. The editing domain is fixed tightly via hydrophobic interactions to the aminoacylation/tRNA-recognition domains, on the side opposite from that in threonyl-tRNA synthetase. A groove formed between the aminoacylation/tRNA-recognition domains and the editing domain appears to be an alternative tRNA-binding site, which might be used for the aminoacylation and/or editing reactions. Actually, the amino acid residues required for the G3:U70 recognition are mapped in this groove. The dimerization domain consists of helical and globular subdomains. The helical subdomain mediates dimerization by forming a helixloop-helix zipper. The globular subdomain, which is important for the aminoacylation and editing activities, has a positively-charged face suitable for tRNA binding.
  • Fa parte di: Proceedings of the National Academy of Sciences of the United States of America, 26 May 2009, Vol.106(21), pp.8489-8494
  • Soggetti: Ligases -- Properties ; Transfer Rna -- Properties ; Protein Structure -- Research
  • Lingua: Inglese
  • Identificativo: ISSN: 00278424 ; DOI: 10.1073/pnas.0901572106

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