Fig. 3: The ϕKp24 helical tail. | Nature Communications

Fig. 3: The ϕKp24 helical tail.

From: High-resolution reconstruction of a Jumbo-bacteriophage infecting capsulated bacteria using hyperbranched tail fibers

Fig. 3

a Top view (top image) and side view (bottom image) orientations of the 3D structure (EMD-14357) of the 3.0 Å helical tail. Each of the six helical strands is colored differently. b Model of tail sheath protein gp118 generated from Alphafold2. Sheath protein gp118 and the inner tube-protein gp119 were fitted into one ring of the ϕKp24 EM map (upper image, top view; lower image, side view). In the bottom panel, the sheath monomer (blue) that originates from the lower layer is shown to allow visualization of the ring-ring interactions. Contacts between three sheath monomers are highlighted from two successive rings (the enlarged rectangular box, lower right panel). c Ribbon diagram of the predicted AlphaFold2 model of the ϕKp24 sheath monomer, gp118. The model consists of two parts: the central sheath (dotted box, orange and dark blue) and an extended outer sheath component (light blue). The lower image is rotated with respect to the upper image by 90° to show the N- terminal extension. d Schematic of the ϕKp24 sheath organization. The ridge, where the three sheath monomers from two layers interact, is shown in a circle.

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