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TitleThree-dimensional reconstructions of the bacteriophage CUS-3 virion reveal a conserved coat protein I-domain but a distinct tailspike receptor-binding domain.
Journal, issue, pagesVirology, Vol. 464-465, Page 55-66, Year 2014
Publish dateJul 18, 2014
AuthorsKristin N Parent / Jinghua Tang / Giovanni Cardone / Eddie B Gilcrease / Mandy E Janssen / Norman H Olson / Sherwood R Casjens / Timothy S Baker /
PubMed AbstractCUS-3 is a short-tailed, dsDNA bacteriophage that infects serotype K1 Escherichia coli. We report icosahedrally averaged and asymmetric, three-dimensional, cryo-electron microscopic reconstructions ...CUS-3 is a short-tailed, dsDNA bacteriophage that infects serotype K1 Escherichia coli. We report icosahedrally averaged and asymmetric, three-dimensional, cryo-electron microscopic reconstructions of the CUS-3 virion. Its coat protein structure adopts the "HK97-fold" shared by other tailed phages and is quite similar to that in phages P22 and Sf6 despite only weak amino acid sequence similarity. In addition, these coat proteins share a unique extra external domain ("I-domain"), suggesting that the group of P22-like phages has evolved over a very long time period without acquiring a new coat protein gene from another phage group. On the other hand, the morphology of the CUS-3 tailspike differs significantly from that of P22 or Sf6, but is similar to the tailspike of phage K1F, a member of the extremely distantly related T7 group of phages. We conclude that CUS-3 obtained its tailspike gene from a distantly related phage quite recently.
External linksVirology / PubMed:25043589 / PubMed Central
MethodsEM (single particle)
Resolution6.8 - 20.0 Å
Structure data

EMDB-5946:
Bacteriophage CUS-3 asymmetric reconstruction
Method: EM (single particle) / Resolution: 20.0 Å

EMDB-5947:
Bacteriophage CUS-3 capsid icosahedral reconstruction
Method: EM (single particle) / Resolution: 6.8 Å

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