In this section
@article{Cheng:2018:10.7554/eLife.42400,
author = {Cheng, K and Wigley, DB},
doi = {10.7554/eLife.42400},
journal = {eLife},
title = {DNA translocation mechanism of an XPD family helicase},
url = {http://dx.doi.org/10.7554/eLife.42400},
volume = {7},
year = {2018}
}
TY - JOUR
AB - 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 (ADP•BeF3), 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 lesionsmight stall at these as the first step in initiating DNA repair. Biochemical data reveal roles for conserved residues that are mutated in human diseases.
AU - Cheng,K
AU - Wigley,DB
DO - 10.7554/eLife.42400
PY - 2018///
SN - 2050-084X
TI - DNA translocation mechanism of an XPD family helicase
T2 - eLife
UR - http://dx.doi.org/10.7554/eLife.42400
UR - https://www.ncbi.nlm.nih.gov/pubmed/30520735
UR - http://hdl.handle.net/10044/1/66819
VL - 7
ER -
Section Manager
Brett Onslow
+44 (0)20 7594 3871
Personal Assistant for the Section of Structural Biology
Kasia Pearce
+44 (0)20 7594 2917
Laboratory Manager
Soo Mei Chee