EMD-1475
Structure of bacteriophage N4
EMD-1475
Single-particle29.0 Å
![EMD-1475](https://www.ebi.ac.uk/emdb/images/entry/EMD-1475/400_1475.gif)
Map released: 31/03/2009
Last modified: 05/05/2009
Sample Organism:
Enterobacteria phage N4
Sample: Bacteriophage N4
Deposition Authors: Choi KH, McPartland J, Kaganman I, Bowman VD, Rothman-Denes LB, Rossmann MG
Sample: Bacteriophage N4
Deposition Authors: Choi KH, McPartland J, Kaganman I, Bowman VD, Rothman-Denes LB, Rossmann MG
Insight into DNA and protein transport in double-stranded DNA viruses: the structure of bacteriophage N4.
Choi KH,
McPartland J,
Kaganman I,
Bowman VD,
Rothman-Denes LB,
Rossmann MG
(2008) J. Mol. Biol. , 378 , 726 - 736
(2008) J. Mol. Biol. , 378 , 726 - 736
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.
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.