Molecular Cell
07 December 2023
Structural insights into the assembly and mechanism of mpox virus DNA polymerase complex F8-A22-E4-H5
Xiaohan Wang1 ,Liangwen Ma1,2 ,Ningning Li1,2,* ,Ning Gao1,2,3,4,*
1.State Key Laboratory of Membrane Biology, Peking-Tsinghua Joint Center for Life Sciences, School of Life Sciences, Peking University, Beijing 100871, China
2.Changping Laboratory, Beijing 102206, China
3.National Biomedical Imaging Center, Peking University, Beijing 100871, China
4.Lead contac
10.1016/j.molcel.2022.11.011
The artwork showcases the architecture of the F8-A22-E4-H5 holoenzyme and highlights its two processivity-enhancing mechanisms. The holoenzyme, depicted by a construction worker, is attached to double-helical green vines by a safety belt and a pair of climbing spikes. The safety belt represents the ring formed by A22-E4, which encircles the single-stranded template DNA upstream F8. The climbing spikes signify the H5 tetramer that attaches to the newly synthesized double-stranded DNA downstream F8.
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