3P0S
Crystal structure of Bombyx mori densovirus 1 capsid
Summary for 3P0S
| Entry DOI | 10.2210/pdb3p0s/pdb |
| Descriptor | Capsid protein VP (1 entity in total) |
| Functional Keywords | icosahedral virus capsid, virus-like particle, capsid protein, beta-barrel, virus |
| Biological source | Bombyx mori densovirus 1 |
| Total number of polymer chains | 1 |
| Total formula weight | 54990.64 |
| Authors | Kaufmann, B.,Rossmann, M.G. (deposition date: 2010-09-29, release date: 2011-03-16, Last modification date: 2024-05-22) |
| Primary citation | Kaufmann, B.,El-Far, M.,Plevka, P.,Bowman, V.D.,Li, Y.,Tijssen, P.,Rossmann, M.G. Structure of Bombyx mori densovirus 1, a silkworm pathogen. J.Virol., 85:4691-4697, 2011 Cited by PubMed Abstract: Bombyx mori densovirus 1 (BmDNV-1), a major pathogen of silkworms, causes significant losses to the silk industry. The structure of the recombinant BmDNV-1 virus-like particle has been determined at 3.1-Å resolution using X-ray crystallography. It is the first near-atomic-resolution structure of a virus-like particle within the genus Iteravirus. The particles consist of 60 copies of the 55-kDa VP3 coat protein. The capsid protein has a β-barrel "jelly roll" fold similar to that found in many diverse icosahedral viruses, including archaeal, bacterial, plant, and animal viruses, as well as other parvoviruses. Most of the surface loops have little structural resemblance to other known parvovirus capsid proteins. In contrast to vertebrate parvoviruses, the N-terminal β-strand of BmDNV-1 VP3 is positioned relative to the neighboring 2-fold related subunit in a "domain-swapped" conformation, similar to findings for other invertebrate parvoviruses, suggesting domain swapping is an evolutionarily conserved structural feature of the Densovirinae. PubMed: 21367906DOI: 10.1128/JVI.02688-10 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.1 Å) |
Structure validation
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