8zmj | pdb_00008zmj

Cryo-EM structure of BMV TLS-TyrRS-YMP(post-1a state)

spinqualitylabelsall models 8zmj, resolution 3.73Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8zmj is a 3 chain structure with sequence from Brome mosaic virus and Phaseolus vulgaris. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.73Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function V7CJ18_PHAVU Publication Abstract from PubMed 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 A, 3.5 A, 3.7 A, and 3.85 A, 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 EF1alpha 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. Structural insights into dynamics of the BMV TLS aminoacylation.,Yang W, Yi R, Yao J, Gao Y, Li S, Gong Q, Zhang K Nat Commun. 2025 Feb 3;16(1):1276. doi: 10.1038/s41467-025-56612-4. PMID:39900568 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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