4ldd: Difference between revisions
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==Crystal Structure of Ebola virus VP40 Hexamer== | ==Crystal Structure of Ebola virus VP40 Hexamer== | ||
<StructureSection load='4ldd' size='340' side='right' caption='[[4ldd]], [[Resolution|resolution]] 3.50Å' scene=''> | <StructureSection load='4ldd' size='340' side='right'caption='[[4ldd]], [[Resolution|resolution]] 3.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4ldd]] is a 3 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4ldd]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Zaire_ebolavirus Zaire ebolavirus]. The October 2014 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Ebola Virus Proteins'' by David Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2014_10 10.2210/rcsb_pdb/mom_2014_10]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LDD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LDD FirstGlance]. <br> | ||
</td></tr> | </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=4ldd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ldd OCA], [https://pdbe.org/4ldd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ldd RCSB], [https://www.ebi.ac.uk/pdbsum/4ldd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ldd ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/VP40_EBOZM VP40_EBOZM] 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.<ref>PMID:15892969</ref> <ref>PMID:16719918</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Ebola Virus Proteins]] | [[Category: Ebola Virus Proteins]] | ||
[[Category: Large Structures]] | |||
[[Category: RCSB PDB Molecule of the Month]] | [[Category: RCSB PDB Molecule of the Month]] | ||
[[Category: | [[Category: Zaire ebolavirus]] | ||
[[Category: Ableson | [[Category: Ableson DM]] | ||
[[Category: Bornholdt | [[Category: Bornholdt ZA]] | ||
[[Category: Saphire | [[Category: Saphire EO]] | ||
Revision as of 13:53, 14 December 2022
Crystal Structure of Ebola virus VP40 HexamerCrystal Structure of Ebola virus VP40 Hexamer
Structural highlights
FunctionVP40_EBOZM 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.[1] [2] Publication Abstract from PubMedProteins, particularly viral proteins, can be multifunctional, but the mechanisms behind multifunctionality are not fully understood. Here, we illustrate through multiple crystal structures, biochemistry, and cellular microscopy that VP40 rearranges into different structures, each with a distinct function required for the ebolavirus life cycle. A butterfly-shaped VP40 dimer traffics to the cellular membrane. Once there, electrostatic interactions trigger rearrangement of the polypeptide into a linear hexamer. These hexamers construct a multilayered, filamentous matrix structure that is critical for budding and resembles tomograms of authentic virions. A third structure of VP40, formed by a different rearrangement, is not involved in virus assembly but instead uniquely binds RNA to regulate viral transcription inside infected cells. These results provide a functional model for ebolavirus matrix assembly and the other roles of VP40 in the virus life cycle and demonstrate how a single wild-type, unmodified polypeptide can assemble into different structures for different functions. PAPERFLICK: Structural Rearrangement of Ebola Virus VP40 Begets Multiple Functions in the Virus Life Cycle.,Bornholdt ZA, Noda T, Abelson DM, Halfmann P, Wood MR, Kawaoka Y, Saphire EO Cell. 2013 Aug 15;154(4):763-74. doi: 10.1016/j.cell.2013.07.015. PMID:23953110[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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