High resolution structure of hexameric herpesvirus DNA-packaging motor elucidates revolving mechanism and ends 20-year fervent debate

In this issue of the Protein&Cell Journal,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 ATPdriven 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.