Electron cryo-microscopy of bacteriophage PR772 reveals the elusive vertex complex and the capsid architecture
Jazyk angličtina Země Anglie, Velká Británie Médium electronic
Typ dokumentu časopisecké články, práce podpořená grantem
Grantová podpora
828-2012-108
Vetenskapsrådet - International
628-2008-1109
Vetenskapsrådet - International
822-2010-6157
Vetenskapsrådet - International
822-2012-5260
Vetenskapsrådet - International
KAW-2011.081
Knut och Alice Wallenbergs Stiftelse - International
ERC-291602
European Research Council - International
349-2011-6488
Vetenskapsrådet - International
2015-06107
Vetenskapsrådet - International
CZ.02.1.01/0.0/0.0/15_003/0000447
European Commission - International
CZ.02.1.01/0.0/0.0/15_003/0000447
European Structural and Investment Funds - International
PubMed
31513011
PubMed Central
PMC6750898
DOI
10.7554/elife.48496
PII: 48496
Knihovny.cz E-zdroje
- Klíčová slova
- Alpatectivirus, Bam35, E. coli, Gammatectivirus, P2, P5, PR772, PRD1, Spikes, Tecitiviridae, Tectivirus, epidemiology, global health, heteropentamer, molecular biophysics, packaging vertex, penton, structural biology, vertex complex,
- MeSH
- bakteriofágy ultrastruktura MeSH
- elektronová kryomikroskopie * MeSH
- kapsida ultrastruktura MeSH
- konformace proteinů MeSH
- počítačové zpracování obrazu MeSH
- Tectiviridae ultrastruktura MeSH
- virové plášťové proteiny ultrastruktura MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- virové plášťové proteiny MeSH
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 Å, while the resolution of the protein capsid is 2.3 Å. 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.
Department of Biochemistry and Biophysics Stockholm University Stockholm Sweden
Institute of Physics ELI Beamlines Academy of Sciences of the Czech Republic Prague Czech Republic
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PDB
6Q5U