4MGU
Crystal structure of Acheta domesticus Densovirus
Summary for 4MGU
| Entry DOI | 10.2210/pdb4mgu/pdb |
| Descriptor | Structural protein VP2, DNA (5'-D(P*TP*TP*T)-3') (2 entities in total) |
| Functional Keywords | virus, jelly-roll, dnv, virus-dna complex, virus/dna |
| Biological source | Acheta domestica densovirus More |
| Total number of polymer chains | 2 |
| Total formula weight | 47715.14 |
| Authors | Meng, G.,Rossmann, M.G. (deposition date: 2013-08-28, release date: 2013-10-30, Last modification date: 2024-02-28) |
| Primary citation | Meng, G.,Zhang, X.,Plevka, P.,Yu, Q.,Tijssen, P.,Rossmann, M.G. The structure and host entry of an invertebrate parvovirus. J.Virol., 87:12523-12530, 2013 Cited by PubMed Abstract: The 3.5-Å resolution X-ray crystal structure of mature cricket parvovirus (Acheta domesticus densovirus [AdDNV]) has been determined. Structural comparisons show that vertebrate and invertebrate parvoviruses have evolved independently, although there are common structural features among all parvovirus capsid proteins. It was shown that raising the temperature of the AdDNV particles caused a loss of their genomes. The structure of these emptied particles was determined by cryo-electron microscopy to 5.5-Å resolution, and the capsid structure was found to be the same as that for the full, mature virus except for the absence of the three ordered nucleotides observed in the crystal structure. The viral protein 1 (VP1) amino termini could be externalized without significant damage to the capsid. In vitro, this externalization of the VP1 amino termini is accompanied by the release of the viral genome. PubMed: 24027306DOI: 10.1128/JVI.01822-13 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.5 Å) |
Structure validation
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