6B0X

Capsid protein and C-terminal part of scaffolding protein in the Staphylococcus aureus phage 80alpha procapsid

Summary for 6B0X

• Entry DOI: 10.2210/pdb6b0x/pdb
• Related: 6B23
• EMDB information: 7030 7035
• Descriptor: Major head protein, Scaffold protein (2 entities in total)
• Functional Keywords: major capsid protein, hk97-like fold, scaffolding protein, procapsid, virus
• Biological source: Staphylococcus phage 80alpha; More
• Total number of polymer chains: 14
• Total formula weight: 421804.77

Authors

Kizziah, J.L.,Dearborn, A.D.,Dokland, T. (deposition date: 2017-09-15, release date: 2017-10-18, Last modification date: 2024-03-13)

Primary citation

Dearborn, A.D.,Wall, E.A.,Kizziah, J.L.,Klenow, L.,Parker, L.K.,Manning, K.A.,Spilman, M.S.,Spear, J.M.,Christie, G.E.,Dokland, T.
Competing scaffolding proteins determine capsid size during mobilization ofStaphylococcus aureuspathogenicity islands.
Elife, 6:-, 2017

PubMed Abstract: pathogenicity islands (SaPIs), such as SaPI1, exploit specific helper bacteriophages, like 80α, for their high frequency mobilization, a process termed 'molecular piracy'. SaPI1 redirects the helper's assembly pathway to form small capsids that can only accommodate the smaller SaPI1 genome, but not a complete phage genome. SaPI1 encodes two proteins, CpmA and CpmB, that are responsible for this size redirection. We have determined the structures of the 80α and SaPI1 procapsids to near-atomic resolution by cryo-electron microscopy, and show that CpmB competes with the 80α scaffolding protein (SP) for a binding site on the capsid protein (CP), and works by altering the angle between capsomers. We probed these interactions genetically and identified second-site suppressors of lethal mutations in SP. Our structures show, for the first time, the detailed interactions between SP and CP in a bacteriophage, providing unique insights into macromolecular assembly processes.

PubMed: 28984245
DOI: 10.7554/eLife.30822

Experimental method

ELECTRON MICROSCOPY (3.8 Å)