Bayfield, Oliver W, Steven, Alasdair C and Antson, Alfred A orcid.org/0000-0002-4533-3816 (2020) Cryo-EM structure in situ reveals a molecular switch that safeguards virus against genome loss. eLife. e55517. ISSN 2050-084X
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 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.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2020 eLife Sciences Publications Ltd. |
Dates: |
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Institution: | The University of York |
Academic Units: | The University of York > Faculty of Sciences (York) > Chemistry (York) |
Depositing User: | Pure (York) |
Date Deposited: | 21 Apr 2020 11:20 |
Last Modified: | 22 Dec 2024 00:14 |
Published Version: | https://doi.org/10.7554/eLife.55517 |
Status: | Published online |
Refereed: | Yes |
Identification Number: | 10.7554/eLife.55517 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:159724 |
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Description: Cryo-EM structure in situ reveals a molecular switch that safeguards virus against genome loss
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