View source for 6lqo


==EBV tegument protein BBRF2/BSRF1 complex==
<StructureSection load='6lqo' size='340' side='right'caption='[[6lqo]], [[Resolution|resolution]] 3.09&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6lqo]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_gammaherpesvirus_4 Human gammaherpesvirus 4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LQO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6LQO FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.0911262&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=6lqo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lqo OCA], [https://pdbe.org/6lqo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6lqo RCSB], [https://www.ebi.ac.uk/pdbsum/6lqo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6lqo ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CEP1_EBVB9 CEP1_EBVB9] Plays a critical role in cytoplasmic virus egress. Participates in the final step of tegumentation and envelope acquisition within the host cytoplasm.[HAMAP-Rule:MF_04038]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Epstein-Barr virus (EBV) is a gamma-herpesvirus associated with the occurrence of several human malignancies. BBRF2 and BSRF1 are two EBV tegument proteins that have been suggested to form a hetero-complex and mediate viral envelopment, but the molecular basis of their interaction and the functional mechanism of this complex remains unknown. Here, we present crystal structures of BBRF2 alone and in complex with BSRF1. BBRF2 has a compact globular architecture featuring a central beta-sheet that is surrounded by 10 helices, it represents a novel fold distinct from other known protein structures. The central portion of BSRF1 folds into two tightly associated antiparallel alpha-helices, forming a composite four-helix bundle with two alpha-helices from BBRF2 via a massive hydrophobic network. In vitro, a BSRF1-derived peptide binds to BBRF2 and reduces the number of viral genome copies in EBV-positive cells. Exogenous BBRF2 and BSRF1 co-localize at the Golgi apparatus. Furthermore, BBRF2 binds capsid and capsid-associated proteins, whereas BSRF1 associates with glycoproteins. These findings indicate that the BBRF2-BSRF1 complex tethers EBV nucleocapsids to the glycoprotein-enriched Golgi membrane, facilitating secondary envelopment.

Structure of Epstein-Barr virus tegument protein complex BBRF2-BSRF1 reveals its potential role in viral envelopment.,He HP, Luo M, Cao YL, Lin YX, Zhang H, Zhang X, Ou JY, Yu B, Chen X, Xu M, Feng L, Zeng MS, Zeng YX, Gao S Nat Commun. 2020 Oct 26;11(1):5405. doi: 10.1038/s41467-020-19259-x. PMID:33106493<ref>PMID:33106493</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6lqo" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Human gammaherpesvirus 4]]
[[Category: Large Structures]]
[[Category: Cao YL]]
[[Category: Gao S]]
[[Category: He HP]]
[[Category: Luo M]]