1Z00
Solution structure of the C-terminal domain of ERCC1 complexed with the C-terminal domain of XPF
Summary for 1Z00
| Entry DOI | 10.2210/pdb1z00/pdb |
| NMR Information | BMRB: 6551 |
| Descriptor | DNA excision repair protein ERCC-1, DNA repair endonuclease XPF (2 entities in total) |
| Functional Keywords | helix-hairpin-helix, hydrolase |
| Biological source | Homo sapiens (human) More |
| Cellular location | Nucleus: P07992 Nucleus (Probable): Q92889 |
| Total number of polymer chains | 2 |
| Total formula weight | 19230.99 |
| Authors | Tripsianes, K.,Folkers, G.,Ab, E.,Das, D.,Odijk, H.,Jaspers, N.G.J.,Hoeijmakers, J.H.J.,Kaptein, R.,Boelens, R. (deposition date: 2005-03-01, release date: 2005-12-20, Last modification date: 2024-05-29) |
| Primary citation | Tripsianes, K.,Folkers, G.,Ab, E.,Das, D.,Odijk, H.,Jaspers, N.G.J.,Hoeijmakers, J.H.J.,Kaptein, R.,Boelens, R. The Structure of the Human ERCC1/XPF Interaction Domains Reveals a Complementary Role for the Two Proteins in Nucleotide Excision Repair Structure, 13:1849-1858, 2005 Cited by PubMed Abstract: The human ERCC1/XPF complex is a structure-specific endonuclease with defined polarity that participates in multiple DNA repair pathways. We report the heterodimeric structure of the C-terminal domains of both proteins responsible for ERCC1/XPF complex formation. Both domains exhibit the double helix-hairpin-helix motif (HhH)2, and they are related by a pseudo-2-fold symmetry axis. In the XPF domain, the hairpin of the second motif is replaced by a short turn. The ERCC1 domain folds properly only in the presence of the XPF domain, which implies a role for XPF as a scaffold for the folding of ERCC1. The intersubunit interactions are largely hydrophobic in nature. NMR titration data show that only the ERCC1 domain of the ERCC1/XPF complex is involved in DNA binding. On the basis of these findings, we propose a model for the targeting of XPF nuclease via ERCC1-mediated interactions in the context of nucleotide excision repair. PubMed: 16338413DOI: 10.1016/j.str.2005.08.014 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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