6FWS
Structure of DinG in complex with ssDNA and ADPBeF
Summary for 6FWS
| Entry DOI | 10.2210/pdb6fws/pdb |
| Descriptor | ATP-dependent DNA helicase DinG, DNA (5'-D(*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*T)-3'), DNA (5'-D(*TP*TP*TP*TP*TP*TP*TP*TP*TP*T)-3'), ... (8 entities in total) |
| Functional Keywords | atp, helicase, translocase, dna binding, dna binding protein |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 4 |
| Total formula weight | 171142.91 |
| Authors | Cheng, K.,Wigley, D. (deposition date: 2018-03-07, release date: 2018-12-19, Last modification date: 2024-05-08) |
| Primary citation | Cheng, K.,Wigley, D.B. DNA translocation mechanism of an XPD family helicase. Elife, 7:-, 2018 Cited by PubMed Abstract: The XPD family of helicases, that includes human disease-related FANCJ, DDX11 and RTEL1, are Superfamily two 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 , 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•BeF), 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. PubMed: 30520735DOI: 10.7554/eLife.42400 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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