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TitleThe asymmetric structure of an icosahedral virus bound to its receptor suggests a mechanism for genome release.
Journal, issue, pagesStructure, Vol. 21, Issue 7, Page 1225-1234, Year 2013
Publish dateJul 2, 2013
AuthorsKyle C Dent / Rebecca Thompson / Amy M Barker / Julian A Hiscox / John N Barr / Peter G Stockley / Neil A Ranson /
PubMed AbstractSimple, spherical RNA viruses have well-understood, symmetric protein capsids, but little structural information is available for their asymmetric components, such as minor proteins and their ...Simple, spherical RNA viruses have well-understood, symmetric protein capsids, but little structural information is available for their asymmetric components, such as minor proteins and their genomes, which are vital for infection. Here, we report an asymmetric structure of bacteriophage MS2, attached to its receptor, the F-pilus. Cryo-electron tomography and subtomographic averaging of such complexes result in a structure containing clear density for the packaged genome, implying that the conformation of the genome is the same in each virus particle. The data also suggest that the single-copy viral maturation protein breaks the symmetry of the capsid, occupying a position that would be filled by a coat protein dimer in an icosahedral shell. This capsomere can thus fulfill its known biological roles in receptor and genome binding and suggests an exit route for the genome during infection.
External linksStructure / PubMed:23810697 / PubMed Central
MethodsEM (subtomogram averaging) / EM (single particle)
Resolution39.0 Å
Structure data

EMDB-2365, PDB-4bp7:
Asymmetric structure of a virus-receptor complex
Method: EM (subtomogram averaging) / Resolution: 39.0 Å

Source
  • Escherichia coli (E. coli)
  • enterobacteria phage ms2 (virus)
KeywordsVIRUS / BACTERIOPHAGE

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