3G21
Crystal structure of the C-terminal domain of the Rous Sarcoma Virus capsid protein: Low pH
Summary for 3G21
| Entry DOI | 10.2210/pdb3g21/pdb |
| Related | 3G0V 3G1G 3G1I 3G26 3G28 3G29 |
| Descriptor | Gag polyprotein, NITRATE ION (3 entities in total) |
| Functional Keywords | alpha-helical bundle, capsid protein, virion, viral protein, retrovirus |
| Biological source | Rous sarcoma virus (RSV-PrC) |
| Cellular location | Matrix protein p19: Virion (Potential). Capsid protein p27: Virion (Potential). Nucleocapsid protein p12: Virion (Potential): P03322 |
| Total number of polymer chains | 1 |
| Total formula weight | 8536.64 |
| Authors | Kingston, R.L. (deposition date: 2009-01-30, release date: 2009-06-02, Last modification date: 2023-11-01) |
| Primary citation | Bailey, G.D.,Hyun, J.K.,Mitra, A.K.,Kingston, R.L. Proton-linked dimerization of a retroviral capsid protein initiates capsid assembly Structure, 17:737-748, 2009 Cited by PubMed Abstract: In mature retroviral particles, the capsid protein (CA) forms a shell encasing the viral replication complex. Human immunodeficiency virus (HIV) CA dimerizes in solution, through its C-terminal domain (CTD), and this interaction is important for capsid assembly. In contrast, other retroviral capsid proteins, including that of Rous sarcoma virus (RSV), do not dimerize with measurable affinity. Here we show, using X-ray crystallography and other biophysical methods, that acidification causes RSV CA to dimerize in a fashion analogous to HIV CA, and that this drives capsid assembly in vitro. A pair of aspartic acid residues, located within the CTD dimer interface, explains why dimerization is linked to proton binding. Our results show that despite overarching structural similarities, the intermolecular forces responsible for forming and stabilizing the retroviral capsid differ markedly across retroviral genera. Our data further suggest that proton binding may regulate RSV capsid assembly, or modulate stability of the assembled capsid. PubMed: 19446529DOI: 10.1016/j.str.2009.03.010 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (0.9 Å) |
Structure validation
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