5W1R
Cryo-EM structure of DNAPKcs
Summary for 5W1R
| Entry DOI | 10.2210/pdb5w1r/pdb |
| EMDB information | 8751 8752 |
| Descriptor | DNA-dependent protein kinase catalytic subunit (1 entity in total) |
| Functional Keywords | dnap, pikk, nhej, v(d)j recombination, dna binding protein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 469673.22 |
| Authors | Sharif, H.,Li, Y.,Wu, H. (deposition date: 2017-06-04, release date: 2017-07-19, Last modification date: 2025-05-21) |
| Primary citation | Sharif, H.,Li, Y.,Dong, Y.,Dong, L.,Wang, W.L.,Mao, Y.,Wu, H. Cryo-EM structure of the DNA-PK holoenzyme. Proc. Natl. Acad. Sci. U.S.A., 114:7367-7372, 2017 Cited by PubMed Abstract: DNA-dependent protein kinase (DNA-PK) is a large protein complex central to the nonhomologous end joining (NHEJ) DNA-repair pathway. It comprises the DNA-PK catalytic subunit (DNA-PKcs) and the heterodimer of DNA-binding proteins Ku70 and Ku80. Here, we report the cryo-electron microscopy (cryo-EM) structures of human DNA-PKcs at 4.4-Å resolution and the DNA-PK holoenzyme at 5.8-Å resolution. The DNA-PKcs structure contains three distinct segments: the N-terminal region with an arm and a bridge, the circular cradle, and the head that includes the kinase domain. Two perpendicular apertures exist in the structure, which are sufficiently large for the passage of dsDNA. The DNA-PK holoenzyme cryo-EM map reveals density for the C-terminal globular domain of Ku80 that interacts with the arm of DNA-PKcs. The Ku80-binding site is adjacent to the previously identified density for the DNA-binding region of the Ku70/Ku80 complex, suggesting concerted DNA interaction by DNA-PKcs and the Ku complex. PubMed: 28652322DOI: 10.1073/pnas.1707386114 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.4 Å) |
Structure validation
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