6P66
The crystal structure of the XPB complex with Bax1 from Archaeoglobus fulgidus at 3.0 Angstrom resolution
Summary for 6P66
| Entry DOI | 10.2210/pdb6p66/pdb |
| Related | 2FWR 2FZ4 2FZL 4ERN 5TNU 6P4F 6P4O 6P4W |
| Descriptor | DNA repair protein RAD25, DNA endonuclease Bax1, CHLORIDE ION, ... (4 entities in total) |
| Functional Keywords | helicase, nuclease, complex, hydrolase |
| Biological source | Archaeoglobus fulgidus DSM 4304 More |
| Total number of polymer chains | 4 |
| Total formula weight | 217494.73 |
| Authors | DuPrez, K.T.,Fan, L.,Hilario, E. (deposition date: 2019-06-03, release date: 2020-06-17, Last modification date: 2024-11-06) |
| Primary citation | DuPrez, K.,He, F.,Chen, Z.,Hilario, E.,Fan, L. Structural basis of the XPB-Bax1 complex as a dynamic helicase-nuclease machinery for DNA repair. Nucleic Acids Res., 48:6326-6339, 2020 Cited by PubMed Abstract: Nucleotide excision repair (NER) is a major DNA repair pathway for a variety of DNA lesions. XPB plays a key role in DNA opening at damage sites and coordinating damage incision by nucleases. XPB is conserved from archaea to human. In archaea, XPB is associated with a nuclease Bax1. Here we report crystal structures of XPB in complex with Bax1 from Archaeoglobus fulgidus (Af) and Sulfolobus tokodaii (St). These structures reveal for the first time four domains in Bax1, which interacts with XPB mainly through its N-terminal domain. A Cas2-like domain likely helps to position Bax1 at the forked DNA allowing the nuclease domain to incise one arm of the fork. Bax1 exists in monomer or homodimer but forms a heterodimer exclusively with XPB. StBax1 keeps StXPB in a closed conformation and stimulates ATP hydrolysis by XPB while AfBax1 maintains AfXPB in the open conformation and reduces its ATPase activity. Bax1 contains two distinguished nuclease active sites to presumably incise DNA damage. Our results demonstrate that protein-protein interactions regulate the activities of XPB ATPase and Bax1 nuclease. These structures provide a platform to understand the XPB-nuclease interactions important for the coordination of DNA unwinding and damage incision in eukaryotic NER. PubMed: 32374860DOI: 10.1093/nar/gkaa324 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
Download full validation report
