In this issue of the Protein & Cell Joual, a research team (from Institute of Biophysics, Chinese Academy of Sciences) led by professors Xiangxi Wang and Zihe Rao report the high-resolution structural and physical properties of the ATP-driven DNA packaging motor of the double-stranded (ds) herpesvirus (Yang et al.2020).The structures of the portal vertex, the channel hub of the DNA packaging motor were also investigated, revealing essential protein-protein interactions in the assembly and maturation of herpesvirus procapsid (Chen et al.2020;Wang et al.2020).Their impressive data clearly demonstrated that the herpesvirus DNA packaging motor forms a hexameric structure and utilizes the revolving mechanism instead of rotation (Fig.1).This is the first paper of its kind, with images in angstromscale resolution, to convincingly elucidate the structure data to end the 20-year debate on whether the structure or the viral DNA packaging motor is pentamer or hexamer, and whether the motion mechanism is rotation or revolution.