2KN7
Structure of the XPF-single strand DNA complex
Summary for 2KN7
Entry DOI | 10.2210/pdb2kn7/pdb |
Related | 1z00 2aq0 |
NMR Information | BMRB: 16449 |
Descriptor | DNA repair endonuclease XPF, DNA (5'-D(*CP*AP*GP*TP*GP*GP*CP*TP*GP*A)-3') (2 entities in total) |
Functional Keywords | ner, xpf/ercc1, hhh, protein-ssdna complex, hydrolase-dna complex, hydrolase/dna |
Biological source | Homo sapiens (human) |
Cellular location | Nucleus (Probable): Q92889 |
Total number of polymer chains | 4 |
Total formula weight | 21016.94 |
Authors | Das, D.,Folkers, G.E.,van Dijk, M.,Jaspers, N.G.J.,Hoeijmakers, J.H.J.,Kaptein, R.,Boelens, R. (deposition date: 2009-08-16, release date: 2010-08-04, Last modification date: 2024-05-01) |
Primary citation | Das, D.,Folkers, G.E.,van Dijk, M.,Jaspers, N.G.J.,Hoeijmakers, J.H.J.,Kaptein, R.,Boelens, R. The structure of the XPF-ssDNA complex underscores the distinct roles of the XPF and ERCC1 helix- hairpin-helix domains in ss/ds DNA recognition Structure, 20:667-675, 2012 Cited by PubMed Abstract: Human XPF/ERCC1 is a structure-specific DNA endonuclease that nicks the damaged DNA strand at the 5' end during nucleotide excision repair. We determined the structure of the complex of the C-terminal domain of XPF with 10 nt ssDNA. A positively charged region within the second helix of the first HhH motif contacts the ssDNA phosphate backbone. One guanine base is flipped out of register and positioned in a pocket contacting residues from both HhH motifs of XPF. Comparison to other HhH-containing proteins indicates a one-residue deletion in the second HhH motif of XPF that has altered the hairpin conformation, thereby permitting ssDNA interactions. Previous nuclear magnetic resonance studies showed that ERCC1 in the XPF-ERCC1 heterodimer can bind dsDNA. Combining the two observations gives a model that underscores the asymmetry of the human XPF/ERCC1 heterodimer in binding at an ss/ds DNA junction. PubMed: 22483113DOI: 10.1016/j.str.2012.02.009 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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