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Nat Commun. 2014 Jul 2;5:4278. doi: 10.1038/ncomms5278.

Protruding knob-like proteins violate local symmetries in an icosahedral marine virus.

Author information

1
Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, Texas 77030, USA.
2
1] Department of Microbiology, Northeastern University, Boston, Massachusetts 02115, USA [2] Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA.
3
Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA.
4
Department of Microbiology, Northeastern University, Boston, Massachusetts 02115, USA.

Abstract

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.

PMID:
24985522
PMCID:
PMC4102127
DOI:
10.1038/ncomms5278
[Indexed for MEDLINE]
Free PMC Article

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