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Updated: Jan 25, 2026
Scalable Isolation and Purification of Extracellular Vesicles from Escherichia coli and Other Bacteria
Published on: October 13, 2021
Crystal structure of a novel ATPase RadD from Escherichia coli
Xiaolin Kuang1,2, Qun Tang1, Yan-Ping Liu1
1National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, People's Republic of China.
Abstract:
The helicase superfamily 2 (SF2) proteins are involved in essentially every step in DNA and RNA metabolism. The radD (yejH) gene, which belongs to SF2, plays an important role in DNA repair. The RadD protein includes all seven conserved SF2 motifs and has shown ATPase activity. Here, we first reported the structure of RadD from Escherichia coli containing two RecA-like domains, a zinc finger motif, and a C-terminal domain. Based on the structure of RadD and other SF2 proteins, we then built a model of the RedD-ATP complex.
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