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DNA translocation mechanism of an XPD family helicase

DOI: 10.7554/eLife.42400 DOI Help

Authors: Kaiying Cheng (Imperial College London) , Dale B. Wigley (Imperial College London)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Elife , VOL 7

State: Published (Approved)
Published: December 2018
Diamond Proposal Number(s): 17221

Open Access Open Access

Abstract: The XPD family of helicases, that includes human disease-related FANCJ, DDX11 and RTEL1, are Superfamily 2 helicases that contain an iron-sulphur cluster domain, translocate on ssDNA in a 5'-3' direction and play important roles in genome stability. Consequently, mutations in several of these family members in eukaryotes cause human diseases. Family members in bacteria, such as the DinG helicase from Escherichia coli, are also involved in DNA repair. Here we present crystal structures of complexes of DinG bound to single-stranded DNA (ssDNA) in the presence and absence of an ATP analogue (ADPÔÇóBeF3), that suggest a mechanism for 5'-3' translocation along the ssDNA substrate. This proposed mechanism has implications for how those enzymes of the XPD family that recognise bulky DNA lesions might stall at these as the first step in initiating DNA repair. Biochemical data reveal roles for conserved residues that are mutated in human diseases.

Subject Areas: Biology and Bio-materials


Instruments: I04-1-Macromolecular Crystallography (fixed wavelength) , I04-Macromolecular Crystallography