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| - | ==EBOLA VIRUS MATRIX PROTEIN VP40 N-TERMINAL DOMAIN IN COMPLEX WITH RNA (HIGH-RESOLUTION VP40[55-194] VARIANT).== | + | |
| - | <StructureSection load='1h2c' size='340' side='right' caption='[[1h2c]], [[Resolution|resolution]] 1.60Å' scene=''> | + | ==Ebola virus matrix protein VP40 N-terminal domain in complex with RNA (High-resolution VP40[55-194] variant).== |
| | + | <StructureSection load='1h2c' size='340' side='right'caption='[[1h2c]], [[Resolution|resolution]] 1.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1h2c]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ebola_virus_sp. Ebola virus sp.] and [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H2C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1H2C FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1h2c]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ebola_virus_sp. Ebola virus sp.] and [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H2C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H2C FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1h2d|1h2d]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</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=1h2c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h2c OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1h2c RCSB], [http://www.ebi.ac.uk/pdbsum/1h2c PDBsum]</span></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=1h2c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h2c OCA], [https://pdbe.org/1h2c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h2c RCSB], [https://www.ebi.ac.uk/pdbsum/1h2c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h2c ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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> | + | [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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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 1h2c" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | [[Category: Ebola virus sp]] | | [[Category: Ebola virus sp]] |
| | [[Category: Escherichia coli]] | | [[Category: Escherichia coli]] |
| - | [[Category: Bracher, A]] | + | [[Category: Large Structures]] |
| - | [[Category: Dessen, A]] | + | [[Category: Bracher A]] |
| - | [[Category: Gomis-Ruth, F X]] | + | [[Category: Dessen A]] |
| - | [[Category: Klenk, H D]] | + | [[Category: Gomis-Ruth FX]] |
| - | [[Category: Weissenhorn, W]] | + | [[Category: Klenk HD]] |
| - | [[Category: Assembly]]
| + | [[Category: Weissenhorn W]] |
| - | [[Category: Budding]]
| + | |
| - | [[Category: Ebola virus]]
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| - | [[Category: Filovirus]]
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| - | [[Category: Matrix protein vp40]]
| + | |
| - | [[Category: Virus-viral protein complex]]
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| - | [[Category: Virus/viral protein]]
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| Structural highlights
Function
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.[1] [2]
Publication Abstract from PubMed
The Ebola virus membrane-associated matrix protein VP40 is thought to be crucial for assembly and budding of virus particles. Here we present the crystal structure of a disk-shaped octameric form of VP40 formed by four antiparallel homodimers of the N-terminal domain. The octamer binds an RNA triribonucleotide containing the sequence 5'-U-G-A-3' through its inner pore surface, and its oligomerization and RNA binding properties are facilitated by two conformational changes when compared to monomeric VP40. The selective RNA interaction stabilizes the ring structure and confers in vitro SDS resistance to octameric VP40. SDS-resistant octameric VP40 is also found in Ebola virus-infected cells, which suggests that VP40 has an additional function in the life cycle of the virus besides promoting virus assembly and budding off the plasma membrane.
The matrix protein VP40 from Ebola virus octamerizes into pore-like structures with specific RNA binding properties.,Gomis-Ruth FX, Dessen A, Timmins J, Bracher A, Kolesnikowa L, Becker S, Klenk HD, Weissenhorn W Structure. 2003 Apr;11(4):423-33. PMID:12679020[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Irie T, Licata JM, Harty RN. Functional characterization of Ebola virus L-domains using VSV recombinants. Virology. 2005 Jun 5;336(2):291-8. PMID:15892969 doi:10.1016/j.virol.2005.03.027
- ↑ Johnson RF, Bell P, Harty RN. Effect of Ebola virus proteins GP, NP and VP35 on VP40 VLP morphology. Virol J. 2006 May 23;3:31. PMID:16719918 doi:10.1186/1743-422X-3-31
- ↑ Gomis-Ruth FX, Dessen A, Timmins J, Bracher A, Kolesnikowa L, Becker S, Klenk HD, Weissenhorn W. The matrix protein VP40 from Ebola virus octamerizes into pore-like structures with specific RNA binding properties. Structure. 2003 Apr;11(4):423-33. PMID:12679020
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