View source for 7n69


==Pre-fusion state 2 of EEEV with localized reconstruction==
<StructureSection load='7n69' size='340' side='right'caption='[[7n69]], [[Resolution|resolution]] 14.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7n69]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Eastern_equine_encephalitis_virus_(strain_Florida_91-469) Eastern equine encephalitis virus (strain Florida 91-469)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7N69 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7N69 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]] 14.1&#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=7n69 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7n69 OCA], [https://pdbe.org/7n69 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7n69 RCSB], [https://www.ebi.ac.uk/pdbsum/7n69 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7n69 ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Alphaviruses can cause severe human arthritis and encephalitis. During virus infection, structural changes of viral glycoproteins in the acidified endosome trigger virus-host membrane fusion for delivery of the capsid core and RNA genome into the cytosol to initiate virus translation and replication. However, mechanisms by which E1 and E2 glycoproteins rearrange in this process remain unknown. Here, we investigate prefusion cryoelectron microscopy (cryo-EM) structures of eastern equine encephalitis virus (EEEV) under acidic conditions. With models fitted into the low-pH cryo-EM maps, we suggest that E2 dissociates from E1, accompanied by a rotation ( approximately 60 degrees ) of the E2-B domain (E2-B) to expose E1 fusion loops. Cryo-EM reconstructions of EEEV bound to a protective antibody at acidic and neutral pH suggest that stabilization of E2-B prevents dissociation of E2 from E1. These findings reveal conformational changes of the glycoprotein spikes in the acidified host endosome. Stabilization of E2-B may provide a strategy for antiviral agent development.

Cryo-EM structures of alphavirus conformational intermediates in low pH-triggered prefusion states.,Chen CL, Klose T, Sun C, Kim AS, Buda G, Rossmann MG, Diamond MS, Klimstra WB, Kuhn RJ Proc Natl Acad Sci U S A. 2022 Jul 26;119(30):e2114119119. doi: , 10.1073/pnas.2114119119. Epub 2022 Jul 22. PMID:35867819<ref>PMID:35867819</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7n69" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Chen C-L]]
[[Category: Klose T]]
[[Category: Kuhn RJ]]