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TitleStructure of the scaffolding protein and portal within the bacteriophage P22 procapsid provides insights into the self-assembly process.
Journal, issue, pagesPLoS Biol, Vol. 23, Issue 4, Page e3003104, Year 2025
Publish dateApr 17, 2025
AuthorsHao Xiao / Wenyuan Chen / Hao Pang / Jing Zheng / Li Wang / Hao Feng / Jingdong Song / Lingpeng Cheng / Hongrong Liu /
PubMed AbstractIn the assembly pathway of tailed double-stranded DNA (dsDNA) bacteriophages and herpesviruses, a procapsid with a dodecameric portal for DNA delivery at a unique vertex is initially formed. ...In the assembly pathway of tailed double-stranded DNA (dsDNA) bacteriophages and herpesviruses, a procapsid with a dodecameric portal for DNA delivery at a unique vertex is initially formed. Appropriate procapsid assembly requires the transient presence of multiple copies of a scaffolding protein (SP), which is absent in the mature virion. However, how the SP contributes to dodecameric portal formation, facilitates portal and coat protein incorporation, and is subsequently released remains unclear because of a lack of structural information. Here, we present the structure of the SP-portal complex within the procapsid of bacteriophage P22 at 3-9 Å resolutions. The AlphaFold2-predicted SP model fits well with the density map of the complex. The SP forms trimers and tetramers that interact to yield a dome-like complex on the portal. Two SP domains mediate multimerization. Each trimer interacts with two neighboring portal subunits. The SP has a loop-hook-like structure that aids in coat protein recruitment during viral assembly. The loops of those SP subunits on the portal are positioned in clefts between adjacent portal subunits. Conformational changes in the portal during phage maturation may trigger the disassembly and release of the SP complex. Our findings provide insights into SP-assisted procapsid assembly in bacteriophage P22 and suggest that this strategy is also implemented by other dsDNA viruses, including herpesviruses.
External linksPLoS Biol / PubMed:40245015 / PubMed Central
MethodsEM (single particle)
Resolution3.0 - 9.2 Å
Structure data

61452

9kyv

EMDB-61452, PDB-9kyv:
The scaffold dimer of phage P22
Method: EM (single particle) / Resolution: 4.9 Å

EMDB-61453: The complete structure of mature P22
Method: EM (single particle) / Resolution: 8.3 Å

EMDB-61454: The overall structure of P22 procapsid
Method: EM (single particle) / Resolution: 9.2 Å

61455

9kyy

EMDB-61455, PDB-9kyy:
The scaffold trimer of phage P22
Method: EM (single particle) / Resolution: 6.9 Å

61456

9kyx

EMDB-61456, PDB-9kyx:
The scaffold tetramer of phage P22
Method: EM (single particle) / Resolution: 6.9 Å

61457

9jg6

EMDB-61457, PDB-9jg6:
The tail-complex structure of phage P22
Method: EM (single particle) / Resolution: 3.21 Å

61460

9jga

EMDB-61460, PDB-9jga:
P22 procapsid portal
Method: EM (single particle) / Resolution: 3.0 Å

61461

9kyw

EMDB-61461: The scaffold c-loop of phage P22
PDB-9kyw: The scaffold C-loop of phage P22
Method: EM (single particle) / Resolution: 6.7 Å

Source
  • salmonella phage p22 (virus)
  • salmonella enterica subsp. enterica serovar typhimurium (bacteria)
KeywordsVIRAL PROTEIN / Complex

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