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TitleNear-atomic structure of a giant virus.
Journal, issue, pagesNat Commun, Vol. 10, Issue 1, Page 388, Year 2019
Publish dateJan 23, 2019
AuthorsQianglin Fang / Dongjie Zhu / Irina Agarkova / Jagat Adhikari / Thomas Klose / Yue Liu / Zhenguo Chen / Yingyuan Sun / Michael L Gross / James L Van Etten / Xinzheng Zhang / Michael G Rossmann /
PubMed AbstractAlthough 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 ...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.
External linksNat Commun / PubMed:30674888 / PubMed Central
MethodsEM (single particle)
Resolution3.5 Å
Structure data

EMDB-0436, PDB-6ncl:
Near-atomic structure of icosahedrally averaged PBCV-1 capsid
Method: EM (single particle) / Resolution: 3.5 Å

Source
  • PBCV-1 (virus)
  • paramecium bursaria chlorella virus 1
KeywordsVIRUS / tape-measure protein / minor capsid proteins / zip protein / giant virus

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