View source for 8zmh


==Cryo-EM structure of Unbound BMV TLS==
<StructureSection load='8zmh' size='340' side='right'caption='[[8zmh]], [[Resolution|resolution]] 4.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8zmh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Brome_mosaic_virus Brome mosaic virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8ZMH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8ZMH FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.6&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8zmh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8zmh OCA], [https://pdbe.org/8zmh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8zmh RCSB], [https://www.ebi.ac.uk/pdbsum/8zmh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8zmh ProSAT]</span></td></tr>
</table>
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== 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<ref>PMID:39900568</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
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</StructureSection>
[[Category: Brome mosaic virus]]
[[Category: Large Structures]]
[[Category: Li S]]
[[Category: Yang W]]
[[Category: Zhang K]]