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TitleProtruding knob-like proteins violate local symmetries in an icosahedral marine virus.
Journal, issue, pagesNat Commun, Vol. 5, Page 4278, Year 2014
Publish dateJul 2, 2014
AuthorsPreeti Gipson / Matthew L Baker / Desislava Raytcheva / Cameron Haase-Pettingell / Jacqueline Piret / Jonathan A King / Wah Chiu /
PubMed AbstractMarine viruses play crucial roles in shaping the dynamics of oceanic microbial communities and in the carbon cycle on Earth. Here we report a 4.7-Å structure of a cyanobacterial virus, Syn5, by ...Marine viruses play crucial roles in shaping the dynamics of oceanic microbial communities and in the carbon cycle on Earth. Here we report a 4.7-Å structure of a cyanobacterial virus, Syn5, by electron cryo-microscopy and modelling. A Cα backbone trace of the major capsid protein (gp39) reveals a classic phage protein fold. In addition, two knob-like proteins protruding from the capsid surface are also observed. Using bioinformatics and structure analysis tools, these proteins are identified to correspond to gp55 and gp58 (each with two copies per asymmetric unit). The non 1:1 stoichiometric distribution of gp55/58 to gp39 breaks all expected local symmetries and leads to non-quasi-equivalence of the capsid subunits, suggesting a role in capsid stabilization. Such a structural arrangement has not yet been observed in any known virus structures.
External linksNat Commun / PubMed:24985522 / PubMed Central
MethodsEM (single particle)
Resolution4.7 Å
Structure data

5954

4bml

EMDB-5954: Protruding Knob-like Proteins Violate Local Symmetries in an Icosahedral Marine Virus
PDB-4bml: C-alpha backbone trace of major capsid protein gp39 found in marine virus Syn5.
Method: EM (single particle) / Resolution: 4.7 Å

Source
  • synechococcus phage syn5 (virus)
KeywordsVIRUS / MARINE VIRUS / OUTER CAPSID PROTEIN / MATURATION

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