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. 2019 Nov;29(11):953-955.
doi: 10.1038/s41422-019-0232-x. Epub 2019 Sep 17.

Structure of the African swine fever virus major capsid protein p72

Qi Liu  1   2 , Bingting Ma  1 , Nianchao Qian  3 , Fan Zhang  3 , Xu Tan  3 , Jianlin Lei  4 , Ye Xiang  5
Affiliations

Structure of the African swine fever virus major capsid protein p72

Qi Liu et al. Cell Res. 2019 Nov.
No abstract available

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Conflict of interest statement

The authors declare no competing interests.

Figures

Fig. 1
Fig. 1
The p72 structure. a Ribbon diagrams showing the structure of the p72 trimer spike. The six jelly-roll barrels and the corresponding insertion domains are colored red, green, yellow, hot pink, cornflower blue and purple, respectively. The side (left) and top (right) views showing the details of the screw propeller-like top, the central β-layer, and the pseudo hexagonal base. b Diagrams showing the topology of p72. The N- and C-terminal jelly-roll barrels and the corresponding insertions are colored red and green, respectively. c Ribbon diagrams showing the structure details of the insertions. d Structure superposition of the ASFV p72 (red) and the faustovirus MCP (PDB: 5J7O) (cornflower blue). The N-terminal residues 1–70 of the ASFV p72 are disordered in the structure. e The fitted p72 trimers (red ribbons) in the cryo-EM map (EMD-8144) of the faustovirus capsid. The map is contoured at 0.7 σ and is shown as semi-transparent solid surface. f The fitted p72 trimer spikes show a zigzag arrangement of their pseudo hexagonal bases. The two jelly-roll domains of the p72 in the center is colored red and green, respectively. The p72 molecules around are all colored light blue
See this image and copyright information in PMC

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