2XD8

Capsid structure of the infectious Prochlorococcus Cyanophage P-SSP7

Summary for 2XD8

• Entry DOI: 10.2210/pdb2xd8/pdb
• EMDB information: 1713
• Descriptor: T7-LIKE CAPSID PROTEIN (1 entity in total)
• Functional Keywords: marine podovirus, t7-like virus, virus
• Biological source: PROCHLOROCOCCUS PHAGE P-SSP7
• Total number of polymer chains: 7
• Total formula weight: 276459.48

Authors

Liu, X.,Zhang, Q.,Murata, K.,Baker, M.L.,Sullivan, M.B.,Fu, C.,Dougherty, M.,Schmid, M.F.,Osburne, M.S.,Chisholm, S.W.,Chiu, W. (deposition date: 2010-04-30, release date: 2010-06-16, Last modification date: 2024-05-08)

Primary citation

Liu, X.,Zhang, Q.,Murata, K.,Baker, M.L.,Sullivan, M.B.,Fu, C.,Dougherty, M.,Schmid, M.F.,Osburne, M.S.,Chisholm, S.W.,Chiu, W.
Structural Changes in a Marine Podovirus Associated with Release of its Genome Into Prochlorococcus
Nat.Struct.Mol.Biol., 17:830-, 2010

PubMed Abstract: Podovirus P-SSP7 infects Prochlorococcus marinus, the most abundant oceanic photosynthetic microorganism. Single-particle cryo-electron microscopy yields icosahedral and asymmetrical structures of infectious P-SSP7 with 4.6-A and 9-A resolution, respectively. The asymmetric reconstruction reveals how symmetry mismatches are accommodated among five of the gene products at the portal vertex. Reconstructions of infectious and empty particles show a conformational change of the 'valve' density in the nozzle, an orientation difference in the tail fibers, a disordering of the C terminus of the portal protein and the disappearance of the core proteins. In addition, cryo-electron tomography of P-SSP7 infecting Prochlorococcus showed the same tail-fiber conformation as that in empty particles. Our observations suggest a mechanism whereby, upon binding to the host cell, the tail fibers induce a cascade of structural alterations of the portal vertex complex that triggers DNA release.

PubMed: 20543830
DOI: 10.1038/NSMB.1823

Experimental method

ELECTRON MICROSCOPY (4.6 Å)