8FQK

Asymmetric unit of HK97 phage prohead I

Summary for 8FQK

• Entry DOI: 10.2210/pdb8fqk/pdb
• Related: 3e8k 3qpr
• EMDB information: 29390
• Descriptor: Scaffolding domain delta (1 entity in total)
• Functional Keywords: prohead i, icosahedral symmetry, hk97, phage, capsid, virus
• Biological source: Escherichia phage HK97
• Total number of polymer chains: 7
• Total formula weight: 296005.17

Authors

Huet, A.,Oh, B.,Maurer, J.,Duda, R.L.,Conway, J.F. (deposition date: 2023-01-06, release date: 2023-06-28, Last modification date: 2024-06-19)

Primary citation

Huet, A.,Oh, B.,Maurer, J.,Duda, R.L.,Conway, J.F.
A symmetry mismatch unraveled: How phage HK97 scaffold flexibly accommodates a 12-fold pore at a 5-fold viral capsid vertex.
Sci Adv, 9:eadg8868-eadg8868, 2023

PubMed Abstract: Tailed bacteriophages and herpesviruses use a transient scaffold to assemble icosahedral capsids with hexameric capsomers on the faces and pentameric capsomers at all but one vertex where a 12-fold portal is thought to nucleate the assembly. How does the scaffold orchestrate this step? We have determined the portal vertex structure of the bacteriophage HK97 procapsid, where the scaffold is a domain of the major capsid protein. The scaffold forms rigid helix-turn-strand structures on the interior surfaces of all capsomers and is further stabilized around the portal, forming trimeric coiled-coil towers, two per surrounding capsomer. These 10 towers bind identically to 10 of 12 portal subunits, adopting a pseudo-12-fold organization that explains how the symmetry mismatch is managed at this early step.

PubMed: 37327331
DOI: 10.1126/sciadv.adg8868

Experimental method

ELECTRON MICROSCOPY (3.5 Å)