PMID:18374942
| Citation |
Choi, KH, McPartland, J, Kaganman, I, Bowman, VD, Rothman-Denes, LB and Rossmann, MG (2008) Insight into DNA and protein transport in double-stranded DNA viruses: the structure of bacteriophage N4. J. Mol. Biol. 378:726-36 |
|---|---|
| Abstract |
Bacteriophage N4 encapsidates a 3500-aa-long DNA-dependent RNA polymerase (vRNAP), which is injected into the host along with the N4 genome upon infection. The three-dimensional structures of wild-type and mutant N4 viruses lacking gp17, gp50, or gp65 were determined by cryoelectron microscopy. The virion has an icosahedral capsid with T=9 quasi-symmetry that encapsidates well-organized double-stranded DNA and vRNAP. The tail, attached at a unique pentameric vertex of the head, consists of a neck, 12 appendages, and six ribbons that constitute a non-contractile sheath around a central tail tube. Comparison of wild-type and mutant virus structures in conjunction with bioinformatics established the identity and virion locations of the major capsid protein (gp56), a decorating protein (gp17), the vRNAP (gp50), the tail sheath (gp65), the appendages (gp66), and the portal protein (gp59). The N4 virion organization provides insight into its assembly and suggests a mechanism for genome and vRNAP transport strategies utilized by this unique system. |
| Links |
PubMed PMC2396777 Online version:10.1016/j.jmb.2008.02.059 |
| Keywords |
Bacteriophage N4/enzymology; Bacteriophage N4/metabolism; Bacteriophage N4/ultrastructure; Cryoelectron Microscopy; DNA, Viral/metabolism; DNA, Viral/ultrastructure; DNA-Directed RNA Polymerases/metabolism; Protein Transport; Viral Proteins/metabolism |
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