Summary information and primary citation

PDB-id
4mgu; SNAP-derived features in text and JSON formats; DNAproDB
Class
virus-DNA
Method
X-ray (3.5 Å)
Summary
Crystal structure of acheta domesticus densovirus
Reference
Meng G, Zhang X, Plevka P, Yu Q, Tijssen P, Rossmann MG (2013): "The structure and host entry of an invertebrate parvovirus." J.Virol., 87, 12523-12530. doi: 10.1128/JVI.01822-13.
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.

Cartoon-block schematics in six views (download the tarball)

PyMOL session file Download PDB file View in 3Dmol.js