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| | ==Cryo-electron tomography and subtomogram averaging of Rous-Sarcoma- Virus deltaMBD virus-like particles== | | ==Cryo-electron tomography and subtomogram averaging of Rous-Sarcoma- Virus deltaMBD virus-like particles== |
| - | <StructureSection load='5a9e' size='340' side='right' caption='[[5a9e]], [[Resolution|resolution]] 7.70Å' scene=''> | + | <SX load='5a9e' size='340' side='right' viewer='molstar' caption='[[5a9e]], [[Resolution|resolution]] 7.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5a9e]] is a 18 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A9E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5A9E FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5a9e]] is a 18 chain structure with sequence from [https://en.wikipedia.org/wiki/Rous_sarcoma_virus Rous sarcoma virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A9E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5A9E FirstGlance]. <br> |
| - | </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=5a9e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a9e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5a9e RCSB], [http://www.ebi.ac.uk/pdbsum/5a9e PDBsum]</span></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]] 7.7Å</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=5a9e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a9e OCA], [https://pdbe.org/5a9e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5a9e RCSB], [https://www.ebi.ac.uk/pdbsum/5a9e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5a9e ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/GAG_RSVP GAG_RSVP]] Capsid protein p27 forms the spherical core of the virus that encapsulates the genomic RNA-nucleocapsid complex (By similarity). The aspartyl protease mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell (By similarity). | + | [https://www.uniprot.org/uniprot/GAG_RSVP GAG_RSVP] Capsid protein p27 forms the spherical core of the virus that encapsulates the genomic RNA-nucleocapsid complex (By similarity). The aspartyl protease mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell (By similarity). |
| | <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 5a9e" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Gag polyprotein 3D structures|Gag polyprotein 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| - | </StructureSection> | + | </SX> |
| - | [[Category: Briggs, J A.G]] | + | [[Category: Large Structures]] |
| - | [[Category: Dick, R A]] | + | [[Category: Rous sarcoma virus]] |
| - | [[Category: Hagen, W J.H]] | + | [[Category: Briggs JAG]] |
| - | [[Category: Schur, F K.M]] | + | [[Category: Dick RA]] |
| - | [[Category: Vogt, V M]] | + | [[Category: Hagen WJH]] |
| - | [[Category: Capsid]] | + | [[Category: Schur FKM]] |
| - | [[Category: Immature retrovirus]] | + | [[Category: Vogt VM]] |
| - | [[Category: Retrovirus]]
| + | |
| - | [[Category: Rous-sarcoma virus]]
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| - | [[Category: Viral protein]]
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| - | [[Category: Virus-like-particle]]
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| Structural highlights
Function
GAG_RSVP Capsid protein p27 forms the spherical core of the virus that encapsulates the genomic RNA-nucleocapsid complex (By similarity). The aspartyl protease mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell (By similarity).
Publication Abstract from PubMed
The polyprotein Gag is the primary structural component of retroviruses. Gag consists of independently folded domains connected by flexible linkers. Interactions between the conserved CA domains of Gag mediate formation of hexameric protein lattices that drive assembly of immature virus particles. Proteolytic cleavage of Gag by the viral protease (PR) is required for maturation of retroviruses from an immature form into an infectious form. Within the assembled Gag lattices of HIV-1 and Mason-Pfizer monkey virus (M-PMV), the C-terminal domain of CA adopts similar quaternary arrangements, while the N-terminal domain of CA is packed in very different manners. Here we have employed cryo-electron tomography and subtomogram averaging to study in vitro assembled, immature virus-like Rous sarcoma virus (RSV) Gag particles, and have determined the structure of CA and the surrounding regions to a resolution of approximately 8 A. We found that the C-terminal domain of RSV CA is arranged similarly to HIV-1 and M-PMV, while the N-terminal domain of CA adopts a novel arrangement in which the upstream p10 domain folds back into the CA lattice. In this position the cleavage site between CA and p10 appears inaccessible to PR. Below CA, an extended density is consistent with the presence of a six-helix bundle formed by the spacer-peptide region. We have also assessed the affect of lattice assembly on proteolytic processing by exogenous PR. The cleavage between p10 and CA is indeed inhibited in the assembled lattice, consistent with structural regulation of proteolytic maturation. IMPORTANCE: Retroviruses first assemble into immature virus particles, requiring interactions between Gag proteins that form a protein layer under the viral membrane. Subsequently, Gag is cleaved by the viral protease enzyme into separate domains, leading to rearrangement of the virus into its infectious form. It is important to understand how Gag is arranged within immature retroviruses, in order to understand how virus assembly occurs, and how maturation takes place. Here we have used techniques called cryo-electron tomography and subtomogram averaging to obtain a detailed structural picture of the CA domains in immature assembled Rous sarcoma virus Gag particles. We find that part of Gag next to CA, called p10, folds back and interacts with CA when Gag assembles. This arrangement is different from that seen in HIV-1 and Mason-Pfizer monkey virus, illustrating further structural diversity of retroviral structures. The structure provides new information on how the virus assembles and undergoes maturation.
The structure of immature-like Rous sarcoma virus Gag particles reveals a structural role for the p10 domain in assembly.,Schur FK, Dick RA, Hagen WJ, Vogt VM, Briggs JA J Virol. 2015 Jul 29. pii: JVI.01502-15. PMID:26223638[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Schur FK, Dick RA, Hagen WJ, Vogt VM, Briggs JA. The structure of immature-like Rous sarcoma virus Gag particles reveals a structural role for the p10 domain in assembly. J Virol. 2015 Jul 29. pii: JVI.01502-15. PMID:26223638 doi:http://dx.doi.org/10.1128/JVI.01502-15
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