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3N7X

Crystal structure of Penaeus stylirostris densovirus capsid

Summary for 3N7X
Entry DOI10.2210/pdb3n7x/pdb
EMDB information1624
DescriptorCapsid protein, CALCIUM ION, MAGNESIUM ION, ... (4 entities in total)
Functional Keywordsicosahedral virus capsid, virus-like particle, capsid protein, beta-barrel, virus, parvovirus, brevidensovirus
Biological sourceInfectious hypodermal and hematopoietic necrosis virus (Penaeus stylirostris densovirus)
Total number of polymer chains1
Total formula weight37613.08
Authors
Kaufmann, B.,Rossmann, M.G. (deposition date: 2010-05-27, release date: 2010-11-17, Last modification date: 2024-04-03)
Primary citationKaufmann, B.,Bowman, V.D.,Li, Y.,Szelei, J.,Waddell, P.J.,Tijssen, P.,Rossmann, M.G.
Structure of Penaeus stylirostris densovirus, a shrimp pathogen.
J.Virol., 84:11289-11296, 2010
Cited by
PubMed Abstract: Penaeus stylirostris densovirus (PstDNV), a pathogen of penaeid shrimp, causes significant damage to farmed and wild shrimp populations. In contrast to other parvoviruses, PstDNV probably has only one type of capsid protein that lacks the phospholipase A2 activity that has been implicated as a requirement during parvoviral host cell infection. The structure of recombinant virus-like particles, composed of 60 copies of the 37.5-kDa coat protein, the smallest parvoviral capsid protein reported thus far, was determined to 2.5-Å resolution by X-ray crystallography. The structure represents the first near-atomic resolution structure within the genus Brevidensovirus. The capsid protein has a β-barrel "jelly roll" motif similar to that found in many icosahedral viruses, including other parvoviruses. The N-terminal portion of the PstDNV coat protein adopts a "domain-swapped" conformation relative to its twofold-related neighbor similar to the insect parvovirus Galleria mellonella densovirus (GmDNV) but in stark contrast to vertebrate parvoviruses. However, most of the surface loops have little structural resemblance to any of the known parvoviral capsid proteins.
PubMed: 20702621
DOI: 10.1128/JVI.01240-10
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.5 Å)
Structure validation

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