8ZMI

Cryo-EM structure of BMV TLS-TyrRS-ATP(Pre-1a state)

8ZMI の概要

• エントリーDOI: 10.2210/pdb8zmi/pdb
• EMDBエントリー: 60248
• 分子名称: tyrosine--tRNA ligase, RNA (169-MER), ADENOSINE-5'-TRIPHOSPHATE (3 entities in total)
• 機能のキーワード: brome osaic virus, trna-like structure, aminoacylation, tyrosyl-trna synthetase, ligase/rna, ligase-rna complex
• 由来する生物種: Phaseolus vulgaris; 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 141220.62

構造登録者

Zhang, K.,Li, S.,Yang, W. (登録日: 2024-05-23, 公開日: 2025-03-12, 最終更新日: 2025-07-23)

主引用文献

Yang, W.,Yi, R.,Yao, J.,Gao, Y.,Li, S.,Gong, Q.,Zhang, K.
Structural insights into dynamics of the BMV TLS aminoacylation.
Nat Commun, 16:1276-1276, 2025

PubMed Abstract: Brome Mosaic Virus (BMV) utilizes a tRNA-like structure (TLS) within its 3' untranslated region to mimic host tRNA functions, aiding aminoacylation and viral replication. This study explores the structural dynamics of BMV TLS interacting with tyrosyl-tRNA synthetase (TyrRS) during aminoacylation. Using cryo-EM, we capture multiple states of the TLS-TyrRS complex, including unbound TLS, pre-1a, post-1a, and catalysis states, with resolutions of 4.6 Å, 3.5 Å, 3.7 Å, and 3.85 Å, respectively. These structural comparisons indicate dynamic changes in both TLS and TyrRS. Upon binding, TLS undergoes dynamic rearrangements, particularly with helices B3 and E pivoting, mediated by the unpaired A36 residue, ensuring effective recognition by TyrRS. The dynamic changes also include a more compact arrangement in the catalytic center of TyrRS and the insertion of 3' CCA end into the enzyme's active site, facilitating two-steps aminoacylation. Enzymatic assays further demonstrated the functional importance of TLS-TyrRS interactions, with mutations in key residues significantly impacting aminoacylation efficiency. Furthermore, Electrophoretic Mobility Shift Assay (EMSA) demonstrated that BMV TLS binds elongation factors EF1α and EF2, suggesting a multifaceted strategy to exploit host translational machinery. These findings not only enhance our knowledge of virus-host interactions but also offer potential targets for antiviral drug development.

PubMed: 39900568
DOI: 10.1038/s41467-025-56612-4

実験手法

ELECTRON MICROSCOPY (3.49 Å)