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TitleA symmetry mismatch unraveled: How phage HK97 scaffold flexibly accommodates a 12-fold pore at a 5-fold viral capsid vertex.
Journal, issue, pagesSci Adv, Vol. 9, Issue 24, Page eadg8868, Year 2023
Publish dateJun 16, 2023
AuthorsAlexis Huet / Bonnie Oh / Josh Maurer / Robert L Duda / James F Conway /
PubMed AbstractTailed 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 ...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.
External linksSci Adv / PubMed:37327331 / PubMed Central
MethodsEM (single particle)
Resolution3.0 - 3.6 Å
Structure data

EMDB-29389: HK97 portal, C12 symmetry
Method: EM (single particle) / Resolution: 3.2 Å

29390

8fqk

EMDB-29390: Prohead I ico symmetry
PDB-8fqk: Asymmetric unit of HK97 phage prohead I
Method: EM (single particle) / Resolution: 3.5 Å

EMDB-29391: HK97 prohead I subsection -regular vertex.
Method: EM (single particle) / Resolution: 3.0 Å

29392

8fql

EMDB-29392: portal vertex of HK97 phage
PDB-8fql: Portal vertex of HK97 phage
Method: EM (single particle) / Resolution: 3.6 Å

Source
  • escherichia phage hk97 (virus)
KeywordsVIRUS / Prohead I / icosahedral symmetry / HK97 / phage / capsid

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