Summary information and primary citation
- PDB-id
-
8wnd;
DSSR-derived features in text and
JSON formats; DNAproDB
- Class
- ligase-RNA
- Method
- X-ray (2.8 Å)
- Summary
- Crystal structure of saccharomyces cerevisiae
isoleucyl-trna synthetase in complex with trna(ile) and
isoleucine
- Reference
-
Chen B, Yi F, Luo Z, Lu F, Liu H, Luo S, Gu Q, Zhou H
(2024): "The
mechanism of discriminative aminoacylation by
isoleucyl-tRNA synthetase based on wobble nucleotide
recognition." Nat Commun,
15, 10817. doi: 10.1038/s41467-024-55183-0.
- 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<sub>Ile</sub> from
tRNA<sub>Met</sub> 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<sub>Ile</sub>, which
induces mutual structural adaptations between ScIleRS and
tRNA<sub>Ile</sub> to achieve a preferable
editing state. C34 of unmodified
tRNA<sub>Ile</sub>(CAU) (behaves like
tRNA<sub>Met</sub>) lacks a relevant H-bond
acceptor, which disrupts key H-bonding interactions and
structural adaptations and suspends the
ScIleRS·tRNA<sub>Ile</sub>(CAU) complex in an
initial non-reactive state. This wobble nucleotide
recognition-based structural adaptation provides
mechanistic insights into selective tRNA aminoacylation by
AARSs.
