Structural highlights
Function
[PORTL_BP234] Forms the portal vertex of the capsid (By similarity). This portal plays critical roles in head assembly, genome packaging, neck/tail attachment, and genome ejection (By similarity). The portal protein multimerizes as a single ring-shaped homododecamer arranged around a central channel (By similarity). Forms the portal vertex of the capsid. This portal plays critical roles in head assembly, genome packaging, neck/tail attachment, and genome ejection (By similarity).[UniProtKB:A0A1L4BKQ4]
Publication Abstract from PubMed
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.
Cryo-EM structure in situ reveals a molecular switch that safeguards virus against genome loss.,Bayfield OW, Steven AC, Antson AA Elife. 2020 Apr 14;9. pii: 55517. doi: 10.7554/eLife.55517. PMID:32286226[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Bayfield OW, Steven AC, Antson AA. Cryo-EM structure in situ reveals a molecular switch that safeguards virus against genome loss. Elife. 2020 Apr 14;9. pii: 55517. doi: 10.7554/eLife.55517. PMID:32286226 doi:http://dx.doi.org/10.7554/eLife.55517
