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2KN7

Structure of the XPF-single strand DNA complex

Summary for 2KN7
Entry DOI10.2210/pdb2kn7/pdb
Related1z00 2aq0
NMR InformationBMRB: 16449
DescriptorDNA repair endonuclease XPF, DNA (5'-D(*CP*AP*GP*TP*GP*GP*CP*TP*GP*A)-3') (2 entities in total)
Functional Keywordsner, xpf/ercc1, hhh, protein-ssdna complex, hydrolase-dna complex, hydrolase/dna
Biological sourceHomo sapiens (human)
Cellular locationNucleus (Probable): Q92889
Total number of polymer chains4
Total formula weight21016.94
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 citationDas, 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: 22483113
DOI: 10.1016/j.str.2012.02.009
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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數據於2024-11-06公開中

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