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TitleStructures of Three Actinobacteriophage Capsids: Roles of Symmetry and Accessory Proteins.
Journal, issue, pagesViruses, Vol. 12, Issue 3, Year 2020
Publish dateMar 8, 2020
AuthorsJennifer Podgorski / Joshua Calabrese / Lauren Alexandrescu / Deborah Jacobs-Sera / Welkin Pope / Graham Hatfull / Simon White /
PubMed AbstractHere, we describe the structure of three actinobacteriophage capsids that infect . The capsid structures were resolved to approximately six angstroms, which allowed confirmation that each ...Here, we describe the structure of three actinobacteriophage capsids that infect . The capsid structures were resolved to approximately six angstroms, which allowed confirmation that each bacteriophage uses the HK97-fold to form their capsid. One bacteriophage, Rosebush, may have a novel variation of the HK97-fold. Four novel accessory proteins that form the capsid head along with the major capsid protein were identified. Two of the accessory proteins were minor capsid proteins and showed some homology, based on bioinformatic analysis, to the TW1 bacteriophage. The remaining two accessory proteins are decoration proteins that are located on the outside of the capsid and do not resemble any previously described bacteriophage decoration protein. SDS-PAGE and mass spectrometry was used to identify the accessory proteins and bioinformatic analysis of the accessory proteins suggest they are used in many actinobacteriophage capsids.
External linksViruses / PubMed:32182721 / PubMed Central
MethodsEM (single particle)
Resolution5.9 - 7.7 Å
Structure data

EMDB-21122:
Actinobacteriophage Rosebush
Method: EM (single particle) / Resolution: 6.7 Å

EMDB-21123:
Actinobacteriophage Patience
Method: EM (single particle) / Resolution: 5.9 Å

EMDB-21124:
Actinobacteriophage Myrna
Method: EM (single particle) / Resolution: 7.7 Å

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