6fws | pdb_00006fws

Structure of DinG in complex with ssDNA and ADPBeF

spinqualitylabelsall models 6fws, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6fws is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ADP, BEF, MG, SF4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [A0A2H4TNL0_ECOLX] DNA-dependent ATPase and 5'-3' DNA helicase.[HAMAP-Rule:MF_02205] Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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