The Structure of an Infectious P22 Virion Shows the Signal for Headful DNA Packaging
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Summary
A 17 angstrom resolution asymmetric reconstruction of the infectious P22 virion reveals that tightly spooled DNA about the portal dodecamer forces a conformation that is significantly different from that observed in isolated portals assembled from ectopically expressed protein.
- Type
- article
- Published
- 2006-06-23
- Cited by
- 320
- References
- 22
- OpenAlex
- https://openalex.org/W2004071147
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:44006470
Keywords
Capsid, DNA, Dodecameric protein, Structural protein, Rolling circle replication
References
- Bacteriophage P22 virion protein which performs an essential early function. II. Characterization of the gene 16 function
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- Phage P22 tailspike protein: crystal structure of the head-binding domain at 2.3 Å, fully refined structure of the endorhamnosidase at 1.56 Å resolution, and the molecular basis of O-antigen recognition and cleavage
- Maturation of phage T7 involves structural modification of both shell and inner core components
- Three-dimensional structure of the bacteriophage P22 tail machine
- Molecular architecture of the prolate head of bacteriophage T4.
- E proteins of bacteriophage P22. I. Identification and ejection from wild-type and defective particles
- Crystal structure of phage P22 tailspike protein complexed with Salmonella sp. O-antigen receptors.
- Bacteriophage P22 portal protein is part of the gauge that regulates packing density of intravirion DNA.
- Conservation of the capsid structure in tailed dsDNA bacteriophages: the pseudoatomic structure of phi29.
- P22 morphogenesis. I: Catalytic scaffolding protein in capsid assembly.
- Symmetry mismatch and DNA packaging in large bacteriophages.
- Structure of the connector of bacteriophage T7 at 8A resolution: structural homologies of a basic component of a DNA translocating machinery.
- Cryoelectron-microscopy image reconstruction of symmetry mismatches in bacteriophage phi29.
- Assembly of a tailed bacterial virus and its genome release studied in three dimensions.
- Coat protein fold and maturation transition of bacteriophage P22 seen at subnanometer resolutions
- Structure of epsilon15 bacteriophage reveals genome organization and DNA packaging/injection apparatus
- Structure of the bacteriophage f29 DNA packaging motor
Cited by
- The structures of bacteriophages K1E and K1-5 explain processive degradation of polysaccharide capsules and evolution of new host specificities.
- The DNA-packaging nanomotor of tailed bacteriophages
- Viral connectors for DNA encapsulation.
- Reconstructing virus structures from nanometer to near-atomic resolutions with cryo-electron microscopy and tomography
- Genetic analysis of structural proteins in the adsorption apparatus of bacteriophage epsilon 15.
- "Push through one-way valve" mechanism of viral DNA packaging.
- Translocation d'acides nucleiques au travers d'une bicouche lipidique : du nanopore au bacteriophage
- The bacteriophage DNA packaging machine.
- Three-Dimensional Asymmetric Reconstruction of Tailed Bacteriophage
- The role of the herpes simplex virus type 1 UL33 protein in DNA packaging
- Role of the Small Terminase Subunit Encoded by Staphylococcus Aureus Pathogenicity Island SaPI1 in Formation of SaPI1 Transducing Particles
- Simulating the Mechanics of Protein-Induced DNA Looping and Protein-Constrained DNA Buckling.
- Gene regulation and function of ICP0 in herpes simplex virus infected cells
- Computational approaches to modeling viral structure and assembly.
- Dynamics of Viral Packaging: Single-Molecule Observations in Multiple Dimensions
- DNA-mediated self-assembly of nanostructures : theory and experiments
- Electrostatic Interactions Stabilizing the I-domain of Bacteriophage P22
- Bacteriophage module reshuffling results in adaptive host range as exemplified by the baseplate model of listerial phage A118.
- Model-Based Statistical Estimation Algorithms For Functional Structural Virology
- Bacteriophage P22 Ejects All of its Internal Proteins Before its Genome
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