Summary information and primary citation

PDB-id
4arc; SNAP-derived features in text and JSON formats; DNAproDB
Class
ligase-RNA
Method
X-ray (2.0 Å)
Summary
Ternary complex of e. coli leucyl-trna synthetase, trna(leu) and leucine in the editing conformation
Reference
Palencia A, Crepin T, Vu MT, Lincecum Jr TL, Martinis SA, Cusack S (2012): "Structural Dynamics of the Aminoacylation and Proofreading Functional Cycle of Bacterial Leucyl-tRNA Synthetase." Nat.Struct.Mol.Biol., 19, 677. doi: 10.1038/NSMB.2317.
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.

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