View source for 9ikc


==Orf virus scaffolding protein Orfv075==
<StructureSection load='9ikc' size='340' side='right'caption='[[9ikc]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9ikc]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Orf_virus_(strain_NZ2) Orf virus (strain NZ2)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9IKC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9IKC 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]] 1.9&#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=9ikc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9ikc OCA], [https://pdbe.org/9ikc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9ikc RCSB], [https://www.ebi.ac.uk/pdbsum/9ikc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9ikc ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q6TW25_ORFV Q6TW25_ORFV] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Capsid-like poxvirus scaffold proteins self-assemble into semi-regular lattice that govern the formation of spherical immature virus particles. The scaffolding is a critical step in virus morphogenesis as exemplified by the drug rifampicin that impairs the recruitment of scaffold onto the viral membrane in vaccinia virus (VACV). Here we report cryo-electron microscopy structure of scaffolding protein Orfv075 of orf virus (ORFV) that causes smallpox-like diseases in sheep, goats and occasionally humans via zoonotic infection. We demonstrate that the regions that are involved in intertrimeric interactions for scaffold assembly are largely conserved in comparison to its VACV orthologue protein D13 whose intermediate assembly structures have been previously characterized. By contrast, less conserved regions are located away from these interfaces, indicating both viruses share similar assembly mechanisms. We also show that the phenylalanine-rich binding site of rifampicin in D13 is conserved in Orfv075, and molecular docking simulation confirms similar binding modes. Our study provides structural basis of scaffolding protein as a target for anti-poxvirus treatment across wide range of poxvirus genera.

Cryo-EM structure of orf virus scaffolding protein orfv075.,Kim S, Ko S, Kim M, Jang Y, Hyun J Biochem Biophys Res Commun. 2024 Oct 8;728:150334. doi: , 10.1016/j.bbrc.2024.150334. Epub 2024 Jun 29. PMID:38968773<ref>PMID:38968773</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9ikc" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Hyun J]]
[[Category: Jang Y]]
[[Category: Kim M]]
[[Category: Kim S]]
[[Category: Ko S]]