1es6

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<StructureSection load='1es6' size='340' side='right'caption='[[1es6]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='1es6' size='340' side='right'caption='[[1es6]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1es6]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ES6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ES6 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1es6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ebola_virus_sp. Ebola virus sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ES6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ES6 FirstGlance]. <br>
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1es6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1es6 OCA], [http://pdbe.org/1es6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1es6 RCSB], [http://www.ebi.ac.uk/pdbsum/1es6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1es6 ProSAT]</span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1es6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1es6 OCA], [https://pdbe.org/1es6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1es6 RCSB], [https://www.ebi.ac.uk/pdbsum/1es6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1es6 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/VP40_EBOG4 VP40_EBOG4]] Promotes virus assembly and budding by interacting with host proteins of the multivesicular body pathway. May facilitate virus budding by interacting with the nucleocapsid and the plasma membrane. Specific interactions with membrane-associated GP and VP24 during the budding process may also occur. The hexamer form seems to be involved in budding. The octamer form binds RNA, and may play a role in genome replication (By similarity).
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[https://www.uniprot.org/uniprot/VP40_EBOZ5 VP40_EBOZ5] Plays an essential role virus particle assembly and budding. Acts by interacting with viral ribonucleocapsid and host members of the ESCRT (endosomal sorting complex required for transport) system such as host VPS4, PDCD6IP/ALIX, NEDD4 or TGS101. The interaction with host E3 ubiquitin ligase SMURF2 also facilitates virus budding. May play a role in immune cell dysfunction by being packaged into exosomes that can decrease the viability of recipient cells (via RNAi suppression and exosome-bystander apoptosis).[UniProtKB:Q05128]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Ebola virus maturation occurs at the plasma membrane of infected cells and involves the clustering of the viral matrix protein VP40 at the assembly site as well as its interaction with the lipid bilayer. Here we report the X-ray crystal structure of VP40 from Ebola virus at 2.0 A resolution. The crystal structure reveals that Ebola virus VP40 is topologically distinct from all other known viral matrix proteins, consisting of two domains with unique folds, connected by a flexible linker. The C-terminal domain, which is absolutely required for membrane binding, contains large hydrophobic patches that may be involved in the interaction with lipid bilayers. Likewise, a highly basic region is shared between the two domains. The crystal structure reveals how the molecule may be able to switch from a monomeric conformation to a hexameric form, as observed in vitro. Its implications for the assembly process are discussed.
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Crystal structure of the matrix protein VP40 from Ebola virus.,Dessen A, Volchkov V, Dolnik O, Klenk HD, Weissenhorn W EMBO J. 2000 Aug 15;19(16):4228-36. PMID:10944105<ref>PMID:10944105</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1es6" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Ebola virus sp]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Dessen, A]]
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[[Category: Dessen A]]
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[[Category: Dolnik, O]]
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[[Category: Dolnik O]]
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[[Category: Klenk, H D]]
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[[Category: Klenk H-D]]
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[[Category: Volchkov, V]]
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[[Category: Volchkov V]]
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[[Category: Weissenhorn, W]]
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[[Category: Weissenhorn W]]
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[[Category: Anti-parallel strand]]
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[[Category: Beta sandwich]]
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[[Category: Beta sheet]]
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[[Category: Helix]]
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[[Category: Viral protein]]
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Current revision

CRYSTAL STRUCTURE OF THE MATRIX PROTEIN OF EBOLA VIRUS

PDB ID 1es6

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