8P26
Crystal structure of Arabidopsis thaliana PAXX
Summary for 8P26
| Entry DOI | 10.2210/pdb8p26/pdb |
| Descriptor | U2 small nuclear ribonucleoprotein auxiliary factor-like protein (2 entities in total) |
| Functional Keywords | dna repair, non-homologous end joining, scaffold, dna binding protein |
| Biological source | Arabidopsis thaliana (thale cress) |
| Total number of polymer chains | 10 |
| Total formula weight | 263445.31 |
| Authors | Ochi, T. (deposition date: 2023-05-15, release date: 2023-06-28, Last modification date: 2023-10-04) |
| Primary citation | Khan, H.,Ochi, T. Plant PAXX has an XLF-like function and stimulates DNA end joining by the Ku-DNA ligase IV/XRCC4 complex. Plant J., 116:58-68, 2023 Cited by PubMed Abstract: Non-homologous end joining (NHEJ) plays a major role in repairing DNA double-strand breaks and is key to genome stability and editing. The minimal core NHEJ proteins, namely Ku70, Ku80, DNA ligase IV and XRCC4, are conserved, but other factors vary in different eukaryote groups. In plants, the only known NHEJ proteins are the core factors, while the molecular mechanism of plant NHEJ remains unclear. Here, we report a previously unidentified plant ortholog of PAXX, the crystal structure of which showed a similar fold to human 'PAXX'. However, plant PAXX has similar molecular functions to human XLF, by directly interacting with Ku70/80 and XRCC4. This suggests that plant PAXX combines the roles of mammalian PAXX and XLF and that these functions merged into a single protein during evolution. This is consistent with a redundant function of PAXX and XLF in mammals. PubMed: 37340932DOI: 10.1111/tpj.16359 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.6 Å) |
Structure validation
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