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Cryo-EM analysis of a viral portal protein in situ reveals a switch in the DNA tunnel

View ORCID ProfileOliver W. Bayfield, View ORCID ProfileAlasdair C. Steven, View ORCID ProfileAlfred A. Antson
doi: https://doi.org/10.1101/713933
Oliver W. Bayfield
aYork Structural Biology Laboratory, Department of Chemistry, University of York, York YO10 5DD, United Kingdom
bLaboratory of Structural Biology Research, National Institute of Arthritis Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, MD 20892, U.S.A.
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  • For correspondence: oliver.bayfield@york.ac.uk fred.antson@york.ac.uk
Alasdair C. Steven
bLaboratory of Structural Biology Research, National Institute of Arthritis Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, MD 20892, U.S.A.
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Alfred A. Antson
aYork Structural Biology Laboratory, Department of Chemistry, University of York, York YO10 5DD, United Kingdom
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  • ORCID record for Alfred A. Antson
  • For correspondence: oliver.bayfield@york.ac.uk fred.antson@york.ac.uk
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Abstract

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 form a ring with a central 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 through its central tunnel, and how these processes can be controlled by capsid and motor proteins. A cryo-EM structure of a portal protein, determined in situ for immature capsids of thermostable bacteriophage P23-45, suggests how domain adjustments can be coupled with a switching of properties of the DNA tunnel. Of particular note is an inversion of the conformation of portal loops which define the tunnel’s constriction, accompanied by a switching of surface properties from hydrophobic to hydrophilic. These observations indicate how translocation of DNA into the viral capsid can be modulated by changes in the properties and size of the central tunnel and how the changing pattern of protein–capsid interactions across a symmetry-mismatched interface can facilitate these dynamic processes.

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Posted July 25, 2019.
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Cryo-EM analysis of a viral portal protein in situ reveals a switch in the DNA tunnel
Oliver W. Bayfield, Alasdair C. Steven, Alfred A. Antson
bioRxiv 713933; doi: https://doi.org/10.1101/713933
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Cryo-EM analysis of a viral portal protein in situ reveals a switch in the DNA tunnel
Oliver W. Bayfield, Alasdair C. Steven, Alfred A. Antson
bioRxiv 713933; doi: https://doi.org/10.1101/713933

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