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. 2018 Sep 10;9:3668. doi: 10.1038/s41467-018-06078-4

Fig. 3.

Fig. 3

The CVSC structure. a Cryo-EM densities of the CVSC surrounding a pentonal vertex. The color scheme is same as in Fig. 1c. The density for the UL25-1 C domain marked by magenta-colored dashed lines, is not observed due to its flexibility in our map. The inset shows the density map (mesh) and atomic model of CVSC which illustrate side chain features. b Pipe-and-plank depictions of the CVSC. The color scheme is same as in Fig. 1c. c Schematic diagram of domain organization of the CVSC five components. d, e Cartoon representation of domain organization of UL17 and two UL25 conformers. Top view of the five-helix bundle (red inset); the left shows the five-helix bundle (colored by residues’ hydrophobic characters: hydrophobic to hydrophilic gradient) viewed along the center of the coiled coil. The blue and yellow insets highlighting the hydrophobic interactions and hydrophobic side chains are shown as sticks. f represents amino acid sequences of the N domain from two UL25 conformers with secondary structural elements labeled; three sets of small β sheets formed separately by two conformers are indicated by three colored lines. The N-terminal 11 residues which are disordered in the structure of UL25-2 are marked by black dots