4AQ7
Ternary complex of E. coli leucyl-tRNA synthetase, tRNA(leu) and leucyl-adenylate analogue in the aminoacylation conformation
Summary for 4AQ7
| Entry DOI | 10.2210/pdb4aq7/pdb |
| Related | 2AJG 2AJH 2AJI 4ARC 4ARI 4AS1 |
| Descriptor | LEUCINE--TRNA LIGASE, E. COLI TRNALEU UAA ISOACCEPTOR, ZINC ION, ... (7 entities in total) |
| Functional Keywords | ligase-rna complex, ligase, nucleotide(atp)-binding, protein biosynthesis, class i aminoacyl-trna synthetase, atp-binding, metal-binding, ligase/rna |
| Biological source | ESCHERICHIA COLI More |
| Cellular location | Cytoplasm: P07813 |
| Total number of polymer chains | 4 |
| Total formula weight | 256271.75 |
| Authors | Palencia, A.,Crepin, T.,Vu, M.T.,Lincecum Jr, T.L.,Martinis, S.A.,Cusack, S. (deposition date: 2012-04-13, 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 Cited by 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: 22683997DOI: 10.1038/NSMB.2317 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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