Backbone structure of the infectious ε15 virus capsid revealed by electron cryomicroscopy

Wen Jiang (), Matthew L. Baker, Joanita Jakana, Peter R. Weigele, Jonathan King and Wah Chiu ()
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Wen Jiang: Markey Center for Structural Biology, Purdue University, West Lafayette, Indiana 47907, USA
Matthew L. Baker: National Center for Macromolecular Imaging, Baylor College of Medicine, Houston, Texas 77030, USA
Joanita Jakana: National Center for Macromolecular Imaging, Baylor College of Medicine, Houston, Texas 77030, USA
Peter R. Weigele: Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA
Jonathan King: Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA
Wah Chiu: National Center for Macromolecular Imaging, Baylor College of Medicine, Houston, Texas 77030, USA

Nature, 2008, vol. 451, issue 7182, 1130-1134

Abstract: Abstract A half-century after the determination of the first three-dimensional crystal structure of a protein1, more than 40,000 structures ranging from single polypeptides to large assemblies have been reported2. The challenge for crystallographers, however, remains the growing of a diffracting crystal. Here we report the 4.5-Å resolution structure of a 22-MDa macromolecular assembly, the capsid of the infectious epsilon15 (ε15) particle, by single-particle electron cryomicroscopy. From this density map we constructed a complete backbone trace of its major capsid protein, gene product 7 (gp7). The structure reveals a similar protein architecture to that of other tailed double-stranded DNA viruses, even in the absence of detectable sequence similarity3,4. However, the connectivity of the secondary structure elements (topology) in gp7 is unique. Protruding densities are observed around the two-fold axes that cannot be accounted for by gp7. A subsequent proteomic analysis of the whole virus identifies these densities as gp10, a 12-kDa protein. Its structure, location and high binding affinity to the capsid indicate that the gp10 dimer functions as a molecular staple between neighbouring capsomeres to ensure the particle’s stability. Beyond ε15, this method potentially offers a new approach for modelling the backbone conformations of the protein subunits in other macromolecular assemblies at near-native solution states.

Date: 2008
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DOI: 10.1038/nature06665

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