Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Electron cryo-microscopy of bacteriophage PR772 reveals the elusive vertex complex and the capsid architecture
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Molecular biophysics.
Stockholm Univ, Dept Biochem & Biophys, Stockholm, Sweden.ORCID iD: 0000-0002-7697-6427
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Molecular biophysics.
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Molecular biophysics.
2019 (English)In: eLIFE, E-ISSN 2050-084X, Vol. 8, article id e48496Article in journal (Refereed) Published
Abstract [en]

Bacteriophage PR772, a member of the Tectiviridae family, has a 70 nm diameter icosahedral protein capsid that encapsulates a lipid membrane, dsDNA, and various internal proteins. An icosahedrally averaged CryoEM reconstruction of the wild-type virion and a localized reconstruction of the vertex region reveal the composition and the structure of the vertex complex along with new protein conformations that play a vital role in maintaining the capsid architecture of the virion. The overall resolution of the virion is 2.75 angstrom, while the resolution of the protein capsid is 2.3 angstrom. The conventional penta-symmetron formed by the capsomeres is replaced by a large vertex complex in the pseudo T = 25 capsid. All the vertices contain the host-recognition protein, P5; two of these vertices show the presence of the receptor-binding protein, P2. The 3D structure of the vertex complex shows interactions with the viral membrane, indicating a possible mechanism for viral infection.

Place, publisher, year, edition, pages
ELIFE SCIENCES PUBLICATIONS LTD , 2019. Vol. 8, article id e48496
National Category
Structural Biology
Identifiers
URN: urn:nbn:se:uu:diva-395312DOI: 10.7554/eLife.48496ISI: 000486655300001PubMedID: 31513011OAI: oai:DiVA.org:uu-395312DiVA, id: diva2:1362230
Funder
Swedish Research Council, 828-2012-108Swedish Research Council, 628-2008-1109Swedish Research Council, 822-2010-6157Swedish Research Council, 822-2012-5260Swedish Research Council, 349-2011-6488Swedish Research Council, 2015-06107Knut and Alice Wallenberg Foundation, KAW-2011.081EU, European Research Council, ERC-291602Available from: 2019-10-18 Created: 2019-10-18 Last updated: 2019-10-18Bibliographically approved

Open Access in DiVA

fulltext(7905 kB)18 downloads
File information
File name FULLTEXT01.pdfFile size 7905 kBChecksum SHA-512
df6d3d6b1f43534da1f4b5e72822e34405fcb3a831b227efbd2e6fadce7d39a23dfb214bfae97d7cf941190e4e6b696a35cc01565b70861180d0fedbcbd7f522
Type fulltextMimetype application/pdf

Other links

Publisher's full textPubMed

Search in DiVA

By author/editor
Reddy, Hemanth K.N.Carroni, MartaHajdu, JSvenda, Martin
By organisation
Molecular biophysics
In the same journal
eLIFE
Structural Biology

Search outside of DiVA

GoogleGoogle Scholar
Total: 18 downloads
The number of downloads is the sum of all downloads of full texts. It may include eg previous versions that are now no longer available

doi
pubmed
urn-nbn

Altmetric score

doi
pubmed
urn-nbn
Total: 20 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf