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6NCL

Near-atomic structure of icosahedrally averaged PBCV-1 capsid

This is a non-PDB format compatible entry.
Summary for 6NCL
Entry DOI10.2210/pdb6ncl/pdb
EMDB information0436
DescriptorP14, P2, P4, ... (15 entities in total)
Functional Keywordstape-measure protein, minor capsid proteins, zip protein, giant virus, virus
Biological sourceParamecium bursaria Chlorella virus 1 (PBCV-1)
More
Total number of polymer chains115
Total formula weight4793078.58
Authors
Fang, Q.,Rossmann, M.G. (deposition date: 2018-12-11, release date: 2019-01-30, Last modification date: 2024-10-16)
Primary citationFang, Q.,Zhu, D.,Agarkova, I.,Adhikari, J.,Klose, T.,Liu, Y.,Chen, Z.,Sun, Y.,Gross, M.L.,Van Etten, J.L.,Zhang, X.,Rossmann, M.G.
Near-atomic structure of a giant virus.
Nat Commun, 10:388-388, 2019
Cited by
PubMed Abstract: Although the nucleocytoplasmic large DNA viruses (NCLDVs) are one of the largest group of viruses that infect many eukaryotic hosts, the near-atomic resolution structures of these viruses have remained unknown. Here we describe a 3.5 Å resolution icosahedrally averaged capsid structure of Paramecium bursaria chlorella virus 1 (PBCV-1). This structure consists of 5040 copies of the major capsid protein, 60 copies of the penton protein and 1800 minor capsid proteins of which there are 13 different types. The minor capsid proteins form a hexagonal network below the outer capsid shell, stabilizing the capsid by binding neighboring capsomers together. The size of the viral capsid is determined by a tape-measure, minor capsid protein of which there are 60 copies in the virion. Homologs of the tape-measure protein and some of the other minor capsid proteins exist in other NCLDVs. Thus, a similar capsid assembly pathway might be used by other NCLDVs.
PubMed: 30674888
DOI: 10.1038/s41467-019-08319-6
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.5 Å)
Structure validation

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