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TitleStructural Analysis of Jumbo Coliphage phAPEC6.
Journal, issue, pagesInt J Mol Sci, Vol. 21, Issue 9, Year 2020
Publish dateApr 28, 2020
AuthorsJeroen Wagemans / Jessica Tsonos / Dominique Holtappels / Kiandro Fortuna / Jean-Pierre Hernalsteens / Henri De Greve / Leandro F Estrozi / Maria Bacia-Verloop / Christine Moriscot / Jean-Paul Noben / Guy Schoehn / Rob Lavigne /
PubMed AbstractThe phAPEC6 genome encodes 551 predicted gene products, with the vast majority (83%) of unknown function. Of these, 62 have been identified as virion-associated proteins by mass spectrometry (ESI- ...The phAPEC6 genome encodes 551 predicted gene products, with the vast majority (83%) of unknown function. Of these, 62 have been identified as virion-associated proteins by mass spectrometry (ESI-MS/MS), including the major capsid protein (Gp225; present in 1620 copies), which shows a HK97 capsid protein-based fold. Cryo-electron microscopy experiments showed that the 350-kbp DNA molecule of virus phAPEC6 is packaged in at least 15 concentric layers in the phage capsid. A capsid inner body rod is also present, measuring about 91 nm by 18 nm and oriented along the portal axis. In the phAPEC6 contractile tail, 25 hexameric stacked rings can be distinguished, built of the identified tail sheath protein (Gp277). Cryo-EM reconstruction reveals the base of the unique hairy fibers observed during an initial transmission electron microscopy (TEM) analysis. These very unusual filaments are ordered at three annular positions along the contractile sheath, as well as around the capsid, and may be involved in host interaction.
External linksInt J Mol Sci / PubMed:32354127 / PubMed Central
MethodsEM (single particle)
Resolution10.0 - 25.0 Å
Structure data

EMDB-10926:
Structure of jumbo coliphage phAPEC6 capsid
Method: EM (single particle) / Resolution: 10.0 Å

EMDB-10929:
3D structure of bacteriophage phAPEC6 tail
Method: EM (single particle) / Resolution: 25.0 Å

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