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| | <SX load='6t63' size='340' side='right' viewer='molstar' caption='[[6t63]], [[Resolution|resolution]] 3.80Å' scene=''> | | <SX load='6t63' size='340' side='right' viewer='molstar' caption='[[6t63]], [[Resolution|resolution]] 3.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6t63]] is a 18 chain structure with sequence from [https://en.wikipedia.org/wiki/Eiav Eiav]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6T63 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6T63 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6t63]] is a 18 chain structure with sequence from [https://en.wikipedia.org/wiki/Equine_infectious_anemia_virus_(CLONE_1369) Equine infectious anemia virus (CLONE 1369)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6T63 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6T63 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gag ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11670 EIAV])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.8Å</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=6t63 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6t63 OCA], [https://pdbe.org/6t63 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6t63 RCSB], [https://www.ebi.ac.uk/pdbsum/6t63 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6t63 ProSAT]</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=6t63 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6t63 OCA], [https://pdbe.org/6t63 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6t63 RCSB], [https://www.ebi.ac.uk/pdbsum/6t63 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6t63 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/GAG_EIAV9 GAG_EIAV9]] Matrix protein p15 forms the outer shell of the core of the virus, lining the inner surface of the viral membrane. Capsid protein p26 forms the conical core of the virus that encapsulates the genomic RNA-nucleocapsid complex. Nucleocapsid protein p11 encapsulates and protects viral dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc fingers (By similarity). p9 plays a role in budding of the assembled particle by interacting with PDCD6IP/AIP1.
| + | [https://www.uniprot.org/uniprot/GAG_EIAV9 GAG_EIAV9] Matrix protein p15 forms the outer shell of the core of the virus, lining the inner surface of the viral membrane. Capsid protein p26 forms the conical core of the virus that encapsulates the genomic RNA-nucleocapsid complex. Nucleocapsid protein p11 encapsulates and protects viral dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc fingers (By similarity). p9 plays a role in budding of the assembled particle by interacting with PDCD6IP/AIP1. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </SX> | | </SX> |
| - | [[Category: Eiav]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Briggs, J A.G]] | + | [[Category: Briggs JAG]] |
| - | [[Category: Broad, A M]] | + | [[Category: Broad AM]] |
| - | [[Category: Dick, R A]] | + | [[Category: Dick RA]] |
| - | [[Category: Feathers, J R]] | + | [[Category: Feathers JR]] |
| - | [[Category: Johnson, M C]] | + | [[Category: Johnson MC]] |
| - | [[Category: Kravchuk, V]] | + | [[Category: Kravchuk V]] |
| - | [[Category: Lyddon, T D]] | + | [[Category: Lyddon TD]] |
| - | [[Category: Morado, D R]] | + | [[Category: Morado DR]] |
| - | [[Category: Perilla, J R]] | + | [[Category: Perilla JR]] |
| - | [[Category: Ricana, C L]] | + | [[Category: Ricana CL]] |
| - | [[Category: Schur, F K.M]] | + | [[Category: Schur FKM]] |
| - | [[Category: Vogt, V M]] | + | [[Category: Vogt VM]] |
| - | [[Category: Xu, C]] | + | [[Category: Xu C]] |
| - | [[Category: Capsid]]
| + | |
| - | [[Category: Equine infectious anemia virus]]
| + | |
| - | [[Category: Gag]]
| + | |
| - | [[Category: Inositolhexakiphosphate]]
| + | |
| - | [[Category: Ip6]]
| + | |
| - | [[Category: Lentivirus]]
| + | |
| - | [[Category: Phytic acid]]
| + | |
| - | [[Category: Retrovirus]]
| + | |
| - | [[Category: Viral protein]]
| + | |
| Structural highlights
Function
GAG_EIAV9 Matrix protein p15 forms the outer shell of the core of the virus, lining the inner surface of the viral membrane. Capsid protein p26 forms the conical core of the virus that encapsulates the genomic RNA-nucleocapsid complex. Nucleocapsid protein p11 encapsulates and protects viral dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc fingers (By similarity). p9 plays a role in budding of the assembled particle by interacting with PDCD6IP/AIP1.
Publication Abstract from PubMed
Retrovirus assembly is driven by the multidomain structural protein Gag. Interactions between the capsid domains (CA) of Gag result in Gag multimerization, leading to an immature virus particle that is formed by a protein lattice based on dimeric, trimeric, and hexameric protein contacts. Among retroviruses the inter- and intra-hexamer contacts differ, especially in the N-terminal sub-domain of CA (CANTD). For HIV-1 the cellular molecule inositol hexakisphosphate (IP6) interacts with and stabilizes the immature hexamer, and is required for production of infectious virus particles. We have used in vitro assembly, cryo-electron tomography and subtomogram averaging, atomistic molecular dynamics simulations and mutational analyses to study the HIV-related lentivirus equine infectious anemia virus (EIAV). In particular, we sought to understand the structural conservation of the immature lentivirus lattice and the role of IP6 in EIAV assembly. Similar to HIV-1, IP6 strongly promoted in vitro assembly of EIAV Gag proteins into virus-like particles (VLPs), which took three morphologically highly distinct forms: narrow tubes, wide tubes, and spheres. Structural characterization of these VLPs to sub-4A resolution unexpectedly showed that all three morphologies are based on an immature lattice with preserved key structural components, highlighting the structural versatility of CA to form immature assemblies. A direct comparison between EIAV and HIV revealed that both lentiviruses maintain similar immature interfaces, which are established by both conserved and non-conserved residues. In both EIAV and HIV-1, IP6 regulates immature assembly via conserved lysine residues within the CACTD and SP. Lastly, we demonstrate that IP6 stimulates in vitro assembly of immature particles of several other retroviruses in the lentivirus genus, suggesting a conserved role for IP6 in lentiviral assembly.
Structures of immature EIAV Gag lattices reveal a conserved role for IP6 in lentivirus assembly.,Dick RA, Xu C, Morado DR, Kravchuk V, Ricana CL, Lyddon TD, Broad AM, Feathers JR, Johnson MC, Vogt VM, Perilla JR, Briggs JAG, Schur FKM PLoS Pathog. 2020 Jan 27;16(1):e1008277. doi: 10.1371/journal.ppat.1008277., eCollection 2020 Jan. PMID:31986188[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Dick RA, Xu C, Morado DR, Kravchuk V, Ricana CL, Lyddon TD, Broad AM, Feathers JR, Johnson MC, Vogt VM, Perilla JR, Briggs JAG, Schur FKM. Structures of immature EIAV Gag lattices reveal a conserved role for IP6 in lentivirus assembly. PLoS Pathog. 2020 Jan 27;16(1):e1008277. doi: 10.1371/journal.ppat.1008277., eCollection 2020 Jan. PMID:31986188 doi:http://dx.doi.org/10.1371/journal.ppat.1008277
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