6fws | pdb_00006fws
Structure of DinG in complex with ssDNA and ADPBeF
Structural highlights
FunctionDING_ECOLI DNA-dependent ATPase and 5'-3' DNA helicase (PubMed:12748189, PubMed:17416902). Can also unwind DNA-RNA hybrid duplexes. Is active on D-loops and R-loops, and on forked structures (PubMed:17416902). May be involved in recombinational DNA repair and the resumption of replication after DNA damage (PubMed:17416902). The redox cluster is involved in DNA-mediated charge-transport signaling between DNA repair proteins from distinct pathways. DinG cooperates at long-range with endonuclease III, a base excision repair enzyme, using DNA charge transport to redistribute to regions of DNA damage (PubMed:24738733).[1] [2] [3] Publication Abstract from PubMedThe 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. DNA translocation mechanism of an XPD family helicase.,Cheng K, Wigley DB Elife. 2018 Dec 6;7. pii: 42400. doi: 10.7554/eLife.42400. PMID:30520735[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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