6ncl | pdb_00006ncl
Near-atomic structure of icosahedrally averaged PBCV-1 capsid
Structural highlights
FunctionP14_PBCV1 One of the minor capsid proteins that constitute a network internal to the major capsid proteins and outside the lipid membrane (PubMed:30674888). The minor capsid protein P14 does not serve a cross-linking function between neighboring capsomers, it may play a role in the viral capsid assembly (PubMed:30674888).[1] Publication Abstract from PubMedAlthough 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 A 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. Near-atomic structure of a giant virus.,Fang Q, Zhu D, Agarkova I, Adhikari J, Klose T, Liu Y, Chen Z, Sun Y, Gross ML, Van Etten JL, Zhang X, Rossmann MG Nat Commun. 2019 Jan 23;10(1):388. doi: 10.1038/s41467-019-08319-6. PMID:30674888[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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