8WND
Crystal structure of Saccharomyces cerevisiae isoleucyl-tRNA synthetase in complex with tRNA(Ile) and isoleucine
Summary for 8WND
| Entry DOI | 10.2210/pdb8wnd/pdb |
| Descriptor | isoleucine--tRNA ligase, tRNA(Ile), ISOLEUCINE, ... (6 entities in total) |
| Functional Keywords | ligaseligase-rna complex, ligase-rna complex, ligase/rna |
| Biological source | Saccharomyces cerevisiae (baker's yeast) More |
| Total number of polymer chains | 4 |
| Total formula weight | 299357.26 |
| Authors | |
| Primary citation | Chen, B.,Yi, F.,Luo, Z.,Lu, F.,Liu, H.,Luo, S.,Gu, Q.,Zhou, H. The mechanism of discriminative aminoacylation by isoleucyl-tRNA synthetase based on wobble nucleotide recognition. Nat Commun, 15:10817-10817, 2024 Cited by PubMed Abstract: The faithful charging of amino acids to cognate tRNAs by aminoacyl-tRNA synthetases (AARSs) determines the fidelity of protein translation. Isoleucyl-tRNA synthetase (IleRS) distinguishes tRNA from tRNA solely based on the nucleotide at wobble position (N34), and a single substitution at N34 could exchange the aminoacylation specificity between two tRNAs. Here, we report the structural and biochemical mechanism of N34 recognition-based tRNA discrimination by Saccharomyces cerevisiae IleRS (ScIleRS). ScIleRS utilizes a eukaryotic/archaeal-specific arginine as the H-bond donor to recognize the common carbonyl group (H-bond acceptor) of various N34s of tRNA, which induces mutual structural adaptations between ScIleRS and tRNA to achieve a preferable editing state. C34 of unmodified tRNA(CAU) (behaves like tRNA) lacks a relevant H-bond acceptor, which disrupts key H-bonding interactions and structural adaptations and suspends the ScIleRS·tRNA(CAU) complex in an initial non-reactive state. This wobble nucleotide recognition-based structural adaptation provides mechanistic insights into selective tRNA aminoacylation by AARSs. PubMed: 39738040DOI: 10.1038/s41467-024-55183-0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
Download full validation report






