9x1v: Difference between revisions

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'''Unreleased structure'''


The entry 9x1v is ON HOLD  until Paper Publication
==Cryo-EM structure of Borna disease virus RNA polymerase complex==
<StructureSection load='9x1v' size='340' side='right'caption='[[9x1v]], [[Resolution|resolution]] 2.72&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9x1v]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Borna_disease_virus-V Borna disease virus-V]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9X1V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9X1V 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]] 2.72&#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=9x1v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9x1v OCA], [https://pdbe.org/9x1v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9x1v RCSB], [https://www.ebi.ac.uk/pdbsum/9x1v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9x1v ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/L_BDVV L_BDVV]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Borna disease virus 1 (BoDV-1) is a neurotropic pathogen that causes severe, often fatal encephalitis, yet effective treatments remain unavailable. As a nuclear-replicating mononegavirus, BoDV-1 employs a minimal L-P polymerase complex. Here, we report cryo-electron microscopy (cryo-EM) structures of the BoDV-1 polymerase in L-alone, apo-L-P, and inhibitor-bound L-P states, revealing the most compact L protein characterized among mononegaviruses. While the catalytic core is conserved, the C-terminal domains are degenerate, with the methyltransferase-like (MTase-like) domain lacking canonical functional motifs. We identify an N-terminal autoinhibitory element (AIE) that is positioned to physically block the template entry tunnel, suggesting an autoinhibition mechanism reminiscent of a "molecular plug." Furthermore, we demonstrate that the inhibitor suramin binds in a specific triple-molecule mode, potentially achieving inhibition by sterically occluding RNA access and allosterically restricting the catalytic core. These findings elucidate the architecture and regulation of the BoDV-1 polymerase, providing a structural framework for rational antiviral design.


Authors: Ma, J., Yang, K., Wu, H., Liang, Z.
Structural mechanism of Borna disease virus 1 RNA polymerase autoinhibition and suramin-mediated inhibition.,Yang K, Wu H, Liang Z, Zou J, Ma J Cell Rep. 2026 May 28;45(6):117462. doi: 10.1016/j.celrep.2026.117462. PMID:42213784<ref>PMID:42213784</ref>


Description: Cryo-EM structure of Borna disease virus RNA polymerase complex
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Liang, Z]]
<div class="pdbe-citations 9x1v" style="background-color:#fffaf0;"></div>
[[Category: Yang, K]]
== References ==
[[Category: Ma, J]]
<references/>
[[Category: Wu, H]]
__TOC__
</StructureSection>
[[Category: Borna disease virus-V]]
[[Category: Large Structures]]
[[Category: Liang Z]]
[[Category: Ma J]]
[[Category: Wu H]]
[[Category: Yang K]]
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