7RWZ

SaPIbov5 procapsid structure including size redirecting protein Ccm

Summary for 7RWZ

• Entry DOI: 10.2210/pdb7rwz/pdb
• EMDB information: 24720
• Descriptor: Cos capsid morphogenesis protein (Ccm), Major capsid protein (2 entities in total)
• Functional Keywords: hk97-like fold, capsid size redirection, major capsid protein, virus
• Biological source: Staphylococcus aureus; More
• Total number of polymer chains: 4
• Total formula weight: 176346.56

Authors

Hawkins, N.C.,Kizziah, J.L.,Dokland, T. (deposition date: 2021-08-20, release date: 2021-11-17, Last modification date: 2024-06-05)

Primary citation

Hawkins, N.C.,Kizziah, J.L.,Penades, J.R.,Dokland, T.
Shape shifter: redirection of prolate phage capsid assembly by staphylococcal pathogenicity islands.
Nat Commun, 12:6408-6408, 2021

PubMed Abstract: Staphylococcus aureus pathogenicity islands (SaPIs) are molecular parasites that hijack helper phages for their transfer. SaPIbov5, the prototypical member of a family of cos type SaPIs, redirects the assembly of ϕ12 helper capsids from prolate to isometric. This size and shape shift is dependent on the SaPIbov5-encoded protein Ccm, a homolog of the ϕ12 capsid protein (CP). Using cryo-electron microscopy, we have determined structures of prolate ϕ12 procapsids and isometric SaPIbov5 procapsids. ϕ12 procapsids have icosahedral end caps with T = 4 architecture and a T = 14 cylindrical midsection, whereas SaPIbov5 procapsids have T = 4 icosahedral architecture. We built atomic models for CP and Ccm, and show that Ccm occupies the pentameric capsomers in the isometric SaPIbov5 procapsids, suggesting that preferential incorporation of Ccm pentamers prevents the cylindrical midsection from forming. Our results highlight that pirate elements have evolved diverse mechanisms to suppress phage multiplication, including the acquisition of phage capsid protein homologs.

PubMed: 34737316
DOI: 10.1038/s41467-021-26759-x

Experimental method

ELECTRON MICROSCOPY (4 Å)