4ARI

Ternary complex of E. coli leucyl-tRNA synthetase, tRNA(leu) and the benzoxaborole AN2679 in the editing conformation

Summary for 4ARI

• Entry DOI: 10.2210/pdb4ari/pdb
• Related: 2AJG 2AJH 2AJI 4AQ7 4ARC 4AS1
• Descriptor: LEUCINE--TRNA LIGASE, TRNA-LEU5 (UAA ISOACEPTOR), GLYCEROL, ... (5 entities in total)
• Functional Keywords: ligase-rna complex, ligase, nucleotide(atp)-binding, protein biosynthesis, class i aminoacyl-trna synthetase, ligase/rna
• Biological source: ESCHERICHIA COLI; More
• Total number of polymer chains: 2
• Total formula weight: 128100.57

Authors

Palencia, A.,Crepin, T.,Vu, M.T.,Lincecum Jr, T.L.,Martinis, S.A.,Cusack, S. (deposition date: 2012-04-24, release date: 2012-06-13, Last modification date: 2023-12-20)

Primary citation

Palencia, A.,Crepin, T.,Vu, M.T.,Lincecum Jr, T.L.,Martinis, S.A.,Cusack, S.
Structural Dynamics of the Aminoacylation and Proofreading Functional Cycle of Bacterial Leucyl-tRNA Synthetase
Nat.Struct.Mol.Biol., 19:677-, 2012

PubMed 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.

PubMed: 22683997
DOI: 10.1038/NSMB.2317

Experimental method

X-RAY DIFFRACTION (2.08 Å)