3TIR
Pseudo-atomic model of the Rous Sarcoma Virus capsid hexamer
Summary for 3TIR
| Entry DOI | 10.2210/pdb3tir/pdb |
| Related | 1EM9 2X8Q 3G21 |
| Descriptor | Rous Sarcoma Virus Capsid Protein p27 (1 entity in total) |
| Functional Keywords | viral capsid protein, viral protein |
| Biological source | Rous sarcoma virus (RSV-PrC) |
| Cellular location | Matrix protein p19: Virion (Potential). Capsid protein p27: Virion (Potential). Nucleocapsid protein p12: Virion (Potential): P03354 |
| Total number of polymer chains | 1 |
| Total formula weight | 24472.23 |
| Authors | Bailey, G.B.,Hyun, J.K.,Mitra, A.K.,Kingston, R.L. (deposition date: 2011-08-21, release date: 2012-04-04, Last modification date: 2023-09-13) |
| Primary citation | Bailey, G.D.,Hyun, J.K.,Mitra, A.K.,Kingston, R.L. A structural model for the generation of continuous curvature on the surface of a retroviral capsid. J.Mol.Biol., 417:212-223, 2012 Cited by PubMed Abstract: 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. PubMed: 22306463DOI: 10.1016/j.jmb.2012.01.014 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (4.1 Å) |
Structure validation
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