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| | ==Pseudo-atomic model of the Rous Sarcoma Virus capsid hexamer== | | ==Pseudo-atomic model of the Rous Sarcoma Virus capsid hexamer== |
| - | <StructureSection load='3tir' size='340' side='right' caption='[[3tir]], [[Resolution|resolution]] 4.10Å' scene=''> | + | <StructureSection load='3tir' size='340' side='right'caption='[[3tir]], [[Resolution|resolution]] 4.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3tir]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rsv-prc Rsv-prc]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TIR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TIR FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3tir]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rsv-prc Rsv-prc]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TIR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TIR FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1em9|1em9]], [[3g21|3g21]], [[2x8q|2x8q]]</td></tr> | + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1em9|1em9]], [[3g21|3g21]], [[2x8q|2x8q]]</div></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CA, gag-pro-pol ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11888 RSV-PrC])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CA, gag-pro-pol ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11888 RSV-PrC])</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=3tir FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tir OCA], [http://pdbe.org/3tir PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3tir RCSB], [http://www.ebi.ac.uk/pdbsum/3tir PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3tir 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=3tir FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tir OCA], [https://pdbe.org/3tir PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tir RCSB], [https://www.ebi.ac.uk/pdbsum/3tir PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tir ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/POL_RSVP POL_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/POL_RSVP POL_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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| | ==See Also== | | ==See Also== |
| - | *[[Virus coat protein|Virus coat protein]] | + | *[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Large Structures]] |
| | [[Category: Rsv-prc]] | | [[Category: Rsv-prc]] |
| | [[Category: Bailey, G B]] | | [[Category: Bailey, G B]] |
| Structural highlights
Function
[POL_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 genome of a retrovirus is surrounded by a convex protein shell, or capsid, that helps facilitate infection. The major part of the capsid surface is formed by interlocking capsid protein (CA) hexamers. We report electron and X-ray crystallographic analysis of a variety of specimens assembled in vitro from Rous sarcoma virus (RSV) CA. These specimens all contain CA hexamers arranged in planar layers, modeling the authentic capsid surface. The specimens differ only in the number of layers incorporated and in the disposition of each layer with respect to its neighbor. The body of each hexamer, formed by the N-terminal domain of CA, is connected to neighboring hexamers through C-terminal domain dimerization. The resulting layer structure is very malleable due to inter-domain flexibility. A helix-capping hydrogen bond between the two domains of RSV CA creates a pivot point, which is central to controlling their relative movement. A similar mechanism for the governance of inter-domain motion was recently described for the human immunodeficiency virus type 1 (HIV-1) capsid, although there is negligible sequence identity between RSV and HIV-1 CA in the region of contact, and the amino acids involved in creating the pivot are not conserved. Our observations allow development of a physically realistic model for the way neighboring hexamers can tilt out of plane, deforming the hexamer layer and generating the continuously curved surfaces that are a feature of all retroviral capsids.
A structural model for the generation of continuous curvature on the surface of a retroviral capsid.,Bailey GD, Hyun JK, Mitra AK, Kingston RL J Mol Biol. 2012 Mar 30;417(3):212-23. Epub 2012 Jan 27. PMID:22306463[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Bailey GD, Hyun JK, Mitra AK, Kingston RL. A structural model for the generation of continuous curvature on the surface of a retroviral capsid. J Mol Biol. 2012 Mar 30;417(3):212-23. Epub 2012 Jan 27. PMID:22306463 doi:10.1016/j.jmb.2012.01.014
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