2xd8
From Proteopedia
Capsid structure of the infectious Prochlorococcus Cyanophage P-SSP7
Structural highlights
FunctionEvolutionary ConservationCheckto colour the structure by Evolutionary Conservation, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedPodovirus 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. Structural changes in a marine podovirus associated with release of its genome into Prochlorococcus.,Liu X, Zhang Q, Murata K, Baker ML, Sullivan MB, Fu C, Dougherty MT, Schmid MF, Osburne MS, Chisholm SW, Chiu W Nat Struct Mol Biol. 2010 Jul;17(7):830-6. Epub 2010 Jun 13. PMID:20543830[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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Categories: Large Structures | Prochlorococcus virus PSSP7 | Baker ML | Chisholm SW | Chiu W | Dougherty M | Fu C | Liu X | Murata K | Osburne MS | Schmid MF | Sullivan MB | Zhang Q