DNA helicases are motor proteins that play essential roles in DNA replication, repair and recombination. In the replicative hexameric helicase, the fundamental reaction is the unwinding of duplex DNA; however, our understanding of this function remains vague due to insufficient structural information. Here, we report two crystal structures of the DnaB-family replicative helicase from Geobacillus kaustophilus HTA426 (GkDnaC) in the apo-form and bound to single-stranded DNA (ssDNA). The research was conducted at the NSRRC beamline BL13B1.

Y. H. Lo, K. L. Tsai, Y. J. Sun, W. T. Chen, C. Y. Huang and C. D. Hsiao