4arc | pdb_00004arc

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

spinqualitylabelsall models 4arc, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4arc is a 2 chain structure with sequence from Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: LEU, MG Related: 2ajg, 2ajh, 2aji, 4aq7 Activity: Leucine--tRNA ligase, with EC number 6.1.1.4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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. Structural dynamics of the aminoacylation and proofreading functional cycle of bacterial leucyl-tRNA synthetase.,Palencia A, Crepin T, Vu MT, Lincecum TL Jr, Martinis SA, Cusack S Nat Struct Mol Biol. 2012 Jun 10. doi: 10.1038/nsmb.2317. PMID:22683997 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also TRNA

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