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TitleCryo-EM structure in situ reveals a molecular switch that safeguards virus against genome loss.
Journal, issue, pagesElife, Vol. 9, Year 2020
Publish dateApr 14, 2020
AuthorsOliver W Bayfield / Alasdair C Steven / Alfred A Antson /
PubMed AbstractThe portal protein is a key component of many double-stranded DNA viruses, governing capsid assembly and genome packaging. Twelve subunits of the portal protein define a tunnel, through which DNA is ...The portal protein is a key component of many double-stranded DNA viruses, governing capsid assembly and genome packaging. Twelve subunits of the portal protein define a tunnel, through which DNA is translocated into the capsid. It is unknown how the portal protein functions as a gatekeeper, preventing DNA slippage, whilst allowing its passage into the capsid, and how these processes are controlled. A cryo-EM structure of the portal protein of thermostable virus P23-45, determined in situ in its procapsid-bound state, indicates a mechanism that naturally safeguards the virus against genome loss. This occurs via an inversion of the conformation of the loops that define the constriction in the central tunnel, accompanied by a hydrophilic-hydrophobic switch. The structure also shows how translocation of DNA into the capsid could be modulated by a changing mode of protein-protein interactions between portal and capsid, across a symmetry-mismatched interface.
External linksElife / PubMed:32286226 / PubMed Central
MethodsEM (single particle)
Resolution3.74 Å
Structure data

4567

6qjt

EMDB-4567: Viral pore protein
PDB-6qjt: Thermophage P23-45 in situ procapsid portal protein
Method: EM (single particle) / Resolution: 3.74 Å

Source
  • Thermus phage P2345 (virus)
  • thermus virus p23-45
KeywordsVIRAL PROTEIN / portal / translocase / motor / pore / bacteriophage / thermophage / caudovirales / siphoviridae / virus

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