Structural dynamics of the aminoacylation and proofreading functional cycle of bacterial leucyl-tRNA synthetase

Andrés Palencia, Thibaut Crépin, Michael T. Vu, Tommie L. Lincecum, Susan A. Martinis, Stephen Cusack

Research output: Contribution to journalArticle

Abstract

Leucyl-tRNA synthetase (LeuRS) produces error-free leucyl-tRNA Leu by coordinating translocation of the 3′ end of (mis-)charged tRNAs from its synthetic site to a separate proofreading site for editing. Here we report cocrystal structures of the Escherichia coli LeuRS-tRNA Leu complex in the aminoacylation or editing conformations, showing that translocation involves correlated rotations of four flexibly linked LeuRS domains. This pivots the tRNA to guide its charged 3′ end from the closed aminoacylation state to the editing site. The editing domain unexpectedly stabilizes the tRNA during aminoacylation, and a large rotation of the leucine-specific domain positions the conserved KMSKS loop to bind the 3′ end of the tRNA, promoting catalysis. Our results give new insight into the structural dynamics of a molecular machine that is essential for accurate protein synthesis.

Original languageEnglish (US)
Pages (from-to)677-684
Number of pages8
JournalNature Structural and Molecular Biology
Volume19
Issue number7
DOIs
StatePublished - Jul 1 2012

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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