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Structure paper

TitlePhi29 assembly intermediates reveal how scaffold interactions with capsid protein drive capsid construction and maturation
Journal, issue, pagesSci Adv, Vol. 11, Year 2025
Publish dateNov 8, 2022 (structure data deposition date)
AuthorsWoodson M / Prokhorov NS / Scott SD / Zhao W / Zhang W / Choi KH / Jardine PJ / Morais MC
External linksSci Adv / Search PubMed
MethodsEM (single particle)
Resolution3.0 - 3.7 Å
Structure data

EMDB-28820: phi-29 prohead MCP gp8 penton maturation intermediate, with associated scaffold gp7 tetramer
Method: EM (single particle) / Resolution: 3.3 Å

EMDB-28821: bacteriophage phi-29 MCP gp-8 penton in intermediate maturation state, with associated scaffold gp7 dimer
Method: EM (single particle) / Resolution: 3.3 Å

28822

8f2m

EMDB-28822, PDB-8f2m:
Phi-29 scaffolding protein bound to intermediate-state MCP
Method: EM (single particle) / Resolution: 3.7 Å

28823

8f2n

EMDB-28823, PDB-8f2n:
Phi-29 partially-expanded fiberless prohead
Method: EM (single particle) / Resolution: 3.0 Å

28824

8f2o

EMDB-28824, PDB-8f2o:
Phi-29 expanded, DNA-packaged fiberless prohead
Method: EM (single particle) / Resolution: 3.0 Å

Source
  • bacillus phage phi29 (virus)
KeywordsVIRUS / bacteriophage / prohead / scaffold / HK97 fold

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