6QJT
Thermophage P23-45 in situ procapsid portal protein
Summary for 6QJT
| Entry DOI | 10.2210/pdb6qjt/pdb |
| EMDB information | 4445 4567 |
| Descriptor | Portal protein (1 entity in total) |
| Functional Keywords | portal, translocase, motor, pore, bacteriophage, thermophage, caudovirales, siphoviridae, virus, viral protein |
| Biological source | Thermus virus P23-45 |
| Total number of polymer chains | 1 |
| Total formula weight | 49714.14 |
| Authors | Bayfield, O.W.,Antson, A.A. (deposition date: 2019-01-24, release date: 2020-03-25, Last modification date: 2024-05-15) |
| Primary citation | Bayfield, O.W.,Steven, A.C.,Antson, A.A. Cryo-EM structure in situ reveals a molecular switch that safeguards virus against genome loss. Elife, 9:-, 2020 Cited by PubMed 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. PubMed: 32286226DOI: 10.7554/eLife.55517 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.74 Å) |
Structure validation
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