5MP9
26S proteasome in presence of ATP (s1)
Summary for 5MP9
| Entry DOI | 10.2210/pdb5mp9/pdb |
| EMDB information | 3534 |
| Descriptor | Proteasome subunit alpha type-1, Proteasome subunit beta type-3, Proteasome subunit beta type-4, ... (23 entities in total) |
| Functional Keywords | macromolecular complex, 26s proteasome, protease, hydrolase |
| Biological source | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) More |
| Cellular location | Cytoplasm : P21243 P25451 P22141 P30656 P23724 P30657 P33299 P40327 P33298 P33297 P23639 Q01939 P23638 P40303 P32379 P40302 P21242 P38624 P25043 |
| Total number of polymer chains | 34 |
| Total formula weight | 1061962.40 |
| Authors | Wehmer, M.,Rudack, T.,Beck, F.,Aufderheide, A.,Pfeifer, G.,Plitzko, J.M.,Foerster, F.,Schulten, K.,Baumeister, W.,Sakata, E. (deposition date: 2016-12-16, release date: 2017-03-08, Last modification date: 2024-05-15) |
| Primary citation | Wehmer, M.,Rudack, T.,Beck, F.,Aufderheide, A.,Pfeifer, G.,Plitzko, J.M.,Forster, F.,Schulten, K.,Baumeister, W.,Sakata, E. Structural insights into the functional cycle of the ATPase module of the 26S proteasome. Proc. Natl. Acad. Sci. U.S.A., 114:1305-1310, 2017 Cited by PubMed Abstract: In eukaryotic cells, the ubiquitin-proteasome system (UPS) is responsible for the regulated degradation of intracellular proteins. The 26S holocomplex comprises the core particle (CP), where proteolysis takes place, and one or two regulatory particles (RPs). The base of the RP is formed by a heterohexameric AAA ATPase module, which unfolds and translocates substrates into the CP. Applying single-particle cryo-electron microscopy (cryo-EM) and image classification to samples in the presence of different nucleotides and nucleotide analogs, we were able to observe four distinct conformational states (s1 to s4). The resolution of the four conformers allowed for the construction of atomic models of the AAA ATPase module as it progresses through the functional cycle. In a hitherto unobserved state (s4), the gate controlling access to the CP is open. The structures described in this study allow us to put forward a model for the 26S functional cycle driven by ATP hydrolysis. PubMed: 28115689DOI: 10.1073/pnas.1621129114 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.1 Å) |
Structure validation
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