The crystal structure of leucyl-tRNA synthetase complexed with tRNA Leu in the post-transfer-editing conformation

Michael Tukalo, Anna Yaremchuk, Ryuya Fukunaga, Shigeyuki Yokoyama, Stephen Cusack

Research output: Contribution to journalArticlepeer-review

Abstract

Leucyl-tRNA synthetase (LeuRS) has a specific post-transfer editing activity directed against mischarged isoleucine and similar noncognate amino acids. We describe the post-transfer-editing and product complexes of Thermus thermophilus LeuRS (LeuRSTT) with tRNALeu at 2.9- to 3.3-Å resolution. In the post-transfer-editing configuration, A76 binds in the editing active site exactly as previously found for the adenosine moiety of a small-molecule editing-substrate analog. The 60 C-terminal residues of LeuRSTT, unseen in previous structures, fold into a compact domain flexibly linked to the rest of the molecule and interacting with the G19-C56 tertiary base pair of tRNALeu. LeuRS recognition of tRNALeu depends essentially on tRNA shape rather than base-specific interactions. The structures show that considerable domain rotations, notably of the editing domain, accompany the tRNA-3′ end dynamics associated successively with aminoacylation, post-transfer editing and product release.

Original languageEnglish (US)
Pages (from-to)923-930
Number of pages8
JournalNature Structural and Molecular Biology
Volume12
Issue number10
DOIs
StatePublished - Oct 2005
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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