3IYJ

Bovine papillomavirus type 1 outer capsid

Summary for 3IYJ

• Entry DOI: 10.2210/pdb3iyj/pdb
• EMDB information: 5155 5156
• Descriptor: Major capsid protein L1 (1 entity in total)
• Functional Keywords: bovine papillomavirus bpv1, major capsid protein l1, single particle cryo-em, high resolution, capsid protein, late protein, virion, virus
• Biological source: Bovine papillomavirus type 1
• Total number of polymer chains: 6
• Total formula weight: 333714.14

Authors

Wolf, M.,Garcea, R.L.,Grigorieff, N.,Harrison, S.C. (deposition date: 2009-12-15, release date: 2010-01-26, Last modification date: 2024-11-06)

Primary citation

Wolf, M.,Garcea, R.L.,Grigorieff, N.,Harrison, S.C.
Subunit interactions in bovine papillomavirus.
Proc.Natl.Acad.Sci.USA, 107:6298-6303, 2010

PubMed Abstract: Papillomaviruses, members of a group of dsDNA viruses associated with epithelial growths and tumors, have compact capsids assembled from 72 pentamers of the protein L1. We have determined the structure of bovine papillomavirus by electron cryomicrosopy (cryoEM), at approximately 3.6 A resolution. The density map, obtained from single-particle analysis of approximately 4,000 particle images, shows the trace of the L1 polypeptide chain and reveals how the N- and C-terminal "arms" of a subunit (extensions from its beta-jelly-roll core) associate with a neighboring pentamer. Critical contacts come from the C-terminal arm, which loops out from the core of the subunit, forms contacts (including a disulfide) with two subunits in a neighboring pentamer, and reinserts into the pentamer from which it emanates. This trace corrects one feature of an earlier model. We discuss implications of the structure for virion assembly and for pathways of infectious viral entry. We suggest that it should be possible to obtain image reconstructions of comparable resolution from cryoEM images of asymmetric particles. From the work on papillomavirus described here, we estimate that such a reconstruction will require about 1.5 million images to achieve the same number of averaged asymmetric units; structural variability will increase this number substantially.

PubMed: 20308582
DOI: 10.1073/pnas.0914604107

Experimental method

ELECTRON MICROSCOPY (4.2 Å)