5LOI
Crystal structure of Myceliophthora thermophila Rad26 (residues 373-841)
Summary for 5LOI
| Entry DOI | 10.2210/pdb5loi/pdb |
| Descriptor | Rad26 (1 entity in total) |
| Functional Keywords | rad26 (atrip), rad3 (atr), dna-damage response (ddr), kinase signaling, signaling protein |
| Biological source | Myceliophthora thermophila ATCC 42464 |
| Total number of polymer chains | 1 |
| Total formula weight | 51698.38 |
| Authors | Andersen, K.R. (deposition date: 2016-08-09, release date: 2017-03-29, Last modification date: 2024-11-13) |
| Primary citation | Andersen, K.R. Insights into Rad3 kinase recruitment from the crystal structure of the DNA damage checkpoint protein Rad26. J. Biol. Chem., 292:8149-8157, 2017 Cited by PubMed Abstract: Metabolic products and environmental factors constantly damage DNA. To protect against these insults and maintain genome integrity, cells have evolved mechanisms to repair DNA lesions. One such mechanism involves Rad3, a master kinase coordinating the DNA damage response. Rad26 is a functional subunit of the Rad3-Rad26 complex and is responsible for bringing the kinase to sites of DNA damage. Here, I present the crystal structure of Rad26 and identify the elements important for recruiting Rad3. The structure suggests that Rad26 is a dimer with a conserved interface in the N-terminal part of the protein. Biochemical data showed that Rad26 uses its C-terminal domain and the flanking kinase-docking motif to bind specific HEAT repeats in Rad3. Analysis of the reconstituted Rad3-Rad26 heterotetrameric complex with electron microscopy enabled me to propose a structural model for its quaternary structure. In conclusion, these results suggest that Rad26 exists as a dimer and provide crucial insight into how Rad3 is recruited and incorporated into the Rad3-Rad26 DNA repair complex. PubMed: 28314775DOI: 10.1074/jbc.M117.780189 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.153 Å) |
Structure validation
Download full validation report
