3H4M
AAA ATPase domain of the proteasome- activating nucleotidase
Summary for 3H4M
| Entry DOI | 10.2210/pdb3h4m/pdb |
| Related | 3H43 3H4P |
| Descriptor | Proteasome-activating nucleotidase, ADENOSINE-5'-DIPHOSPHATE (2 entities in total) |
| Functional Keywords | atpase, proteasome, pan, atp-binding, nucleotide-binding, hydrolase |
| Biological source | Methanocaldococcus jannaschii (Methanococcus jannaschii) |
| Cellular location | Cytoplasm: Q58576 |
| Total number of polymer chains | 3 |
| Total formula weight | 97387.51 |
| Authors | Jeffrey, P.,Zhang, F.,Hu, M.,Tian, G.,Zhang, P.,Finley, D.,Shi, Y. (deposition date: 2009-04-20, release date: 2009-06-09, Last modification date: 2024-02-21) |
| Primary citation | Zhang, F.,Hu, M.,Tian, G.,Zhang, P.,Finley, D.,Jeffrey, P.D.,Shi, Y. Structural Insights into the Regulatory Particle of the Proteasome from Methanocaldococcus jannaschii. Mol.Cell, 34:473-484, 2009 Cited by PubMed Abstract: Eukaryotic proteasome consists of a core particle (CP), which degrades unfolded protein, and a regulatory particle (RP), which is responsible for recognition, ATP-dependent unfolding, and translocation of polyubiquitinated substrate protein. In the archaea Methanocaldococcus jannaschii, the RP is a homohexameric complex of proteasome-activating nucleotidase (PAN). Here, we report the crystal structures of essential elements of the archaeal proteasome: the CP, the ATPase domain of PAN, and a distal subcomplex that is likely the first to encounter substrate. The distal subcomplex contains a coiled-coil segment and an OB-fold domain, both of which appear to be conserved in the eukaryotic proteasome. The OB domains of PAN form a hexameric ring with a 13 A pore, which likely constitutes the outermost constriction of the substrate translocation channel. These studies reveal structural codes and architecture of the complete proteasome, identify potential substrate-binding sites, and uncover unexpected asymmetry in the RP of archaea and eukaryotes. PubMed: 19481527DOI: 10.1016/j.molcel.2009.04.021 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.106 Å) |
Structure validation
Download full validation report
