Aminoacylation complex structures of leucyl-tRNA synthetase and tRNA Leu reveal two modes of discriminator-base recognition

Ryuya Fukunaga, Shigeyuki Yokoyama

Research output: Contribution to journalArticle

Abstract

Leucyl-tRNA synthetase (LeuRS) specifically recognizes the characteristic long variable arm and the discriminator base, A73, of tRNALeu in archaea and eukarya. The LeuRS 'editing domain' hydrolyzes misformed noncognate aminoacyl-tRNA. Here we report the crystal structure of the archaeal Pyrococcus horikoshii LeuRS-tRNALeu complex. The protruding C-terminal domain of LeuRS specifically recognizes the bases at the tip of the long variable arm. The editing domain swings from its tRNA-free position to avoid clashing with the tRNA. Consequently the tRNA CCA end can bend and reach the aminoacylation active site. The tRNA 3′ region assumes two distinct conformations that allow A73 to be specifically recognized in different ways. One conformation is the canonical 'aminoacylation state.' The other conformation seems to be the 'intermediate state,' where the misaminoacylated 3′ end has partially relocated to the editing domain.

Original languageEnglish (US)
Pages (from-to)915-922
Number of pages8
JournalNature Structural and Molecular Biology
Volume12
Issue number10
DOIs
StatePublished - Oct 1 2005
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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