期刊
NATURE STRUCTURAL & MOLECULAR BIOLOGY
卷 17, 期 7, 页码 830-U76出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.1823
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资金
- US National Institutes of Health [P41RR002250, R01GM079429]
- US National Science Foundation [IIS-0705644]
- Robert Welch Foundation [Q1242]
- US Department of Energy
- Gordon and Betty Moore Foundation
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-angstrom and 9-angstrom 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.
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