Structural and functional studies of a large winged Z-DNA-binding domain of Danio rerio protein kinase PKZ
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Published on: March 5, 2019
Vinod Kumar Subramani1, Doyoun Kim1, Kyunghee Yun1
1Department of Molecular Cell Biology, Sungkyunkwan University School of Medicine, Suwon, Korea.
Abstract:
The Z-DNA-binding domain of PKZ from zebrafish (Danio rerio; drZαPKZ ) contains the largest β-wing among known Z-DNA-binding domains. To elucidate the functional implication of the β-wing, we solved the crystal structure of apo-drZαPKZ . Structural comparison with its Z-DNA-bound form revealed a large conformational change within the β-wing during Z-DNA binding. Biochemical studies of protein mutants revealed that two basic residues in the β-wing are responsible for Z-DNA recognition as well as fast B-Z transition. Therefore, the extra basic residues in the β-wing of drZαPKZ are necessary for the fast B-Z transition activity.
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