Spanish Ministry of Science, Innovation, and Universities
BFU 2014-54181
Spain
Spanish Ministry of Science, Innovation, and Universities
BFU2014-53550-P
Spain
Spanish Ministry of Science, Innovation, and Universities
BFU2017-83720-P
Spain
Spanish Ministry of Science, Innovation, and Universities
MDM-2014-0435
Spain
Spanish Ministry of Science, Innovation, and Universities
SEV-2013-0347
Spain
Spanish Ministry of Science, Innovation, and Universities
RYC-2011-09071
Spain
European Commission
653706
Citation
Journal: Nat Commun / Year: 2019 Title: Structures of T7 bacteriophage portal and tail suggest a viral DNA retention and ejection mechanism. Authors: Ana Cuervo / Montserrat Fàbrega-Ferrer / Cristina Machón / José Javier Conesa / Francisco J Fernández / Rosa Pérez-Luque / Mar Pérez-Ruiz / Joan Pous / M Cristina Vega / José L Carrascosa / Miquel Coll / Abstract: Double-stranded DNA bacteriophages package their genome at high pressure inside a procapsid through the portal, an oligomeric ring protein located at a unique capsid vertex. Once the DNA has been ...Double-stranded DNA bacteriophages package their genome at high pressure inside a procapsid through the portal, an oligomeric ring protein located at a unique capsid vertex. Once the DNA has been packaged, the tail components assemble on the portal to render the mature infective virion. The tail tightly seals the ejection conduit until infection, when its interaction with the host membrane triggers the opening of the channel and the viral genome is delivered to the host cell. Using high-resolution cryo-electron microscopy and X-ray crystallography, here we describe various structures of the T7 bacteriophage portal and fiber-less tail complex, which suggest a possible mechanism for DNA retention and ejection: a portal closed conformation temporarily retains the genome before the tail is assembled, whereas an open portal is found in the tail. Moreover, a fold including a seven-bladed β-propeller domain is described for the nozzle tail protein.
A: Portal protein B: Portal protein C: Portal protein D: Portal protein E: Portal protein F: Portal protein G: Portal protein H: Portal protein I: Portal protein J: Portal protein K: Portal protein L: Portal protein
Resolution: 3.6→49.23 Å / Cor.coef. Fo:Fc: 0.91 / Cor.coef. Fo:Fc free: 0.88 / SU B: 212.101 / SU ML: 1.223 / Cross valid method: THROUGHOUT / ESU R Free: 0.942 / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.33441
4317
5 %
RANDOM
Rwork
0.28393
-
-
-
obs
0.28643
82010
89.66 %
-
Solvent computation
Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å
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