5T0C
Structural basis for dynamic regulation of the human 26S proteasome
This is a non-PDB format compatible entry.
Summary for 5T0C
| Entry DOI | 10.2210/pdb5t0c/pdb |
| Related | 5T0G 5T0H 5T0I 5T0J |
| EMDB information | 8332 8333 8334 8335 8336 8337 |
| Descriptor | 26S proteasome non-ATPase regulatory subunit 1, 26S proteasome non-ATPase regulatory subunit 8, 26S proteasome complex subunit DSS1, ... (35 entities in total) |
| Functional Keywords | ubiquitin-proteasome system, aaa-atpase, hydrolase |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 64 |
| Total formula weight | 2548853.32 |
| Authors | Chen, S.,Wu, J.,Lu, Y.,Ma, Y.B.,Lee, B.H.,Yu, Z.,Ouyang, Q.,Finley, D.,Kirschner, M.W.,Mao, Y. (deposition date: 2016-08-15, release date: 2016-10-19, Last modification date: 2024-11-06) |
| Primary citation | Chen, S.,Wu, J.,Lu, Y.,Ma, Y.B.,Lee, B.H.,Yu, Z.,Ouyang, Q.,Finley, D.J.,Kirschner, M.W.,Mao, Y. Structural basis for dynamic regulation of the human 26S proteasome. Proc.Natl.Acad.Sci.USA, 113:12991-12996, 2016 Cited by PubMed Abstract: The proteasome is the major engine of protein degradation in all eukaryotic cells. At the heart of this machine is a heterohexameric ring of AAA (ATPases associated with diverse cellular activities) proteins that unfolds ubiquitylated target proteins that are concurrently translocated into a proteolytic chamber and degraded into peptides. Using cryoelectron microscopy, we determined a near-atomic-resolution structure of the 2.5-MDa human proteasome in its ground state, as well as subnanometer-resolution structures of the holoenzyme in three alternative conformational states. The substrate-unfolding AAA-ATPase channel is narrowed by 10 inward-facing pore loops arranged into two helices that run in parallel with each other, one hydrophobic in character and the other highly charged. The gate of the core particle was unexpectedly found closed in the ground state and open in only one of the alternative states. Coordinated, stepwise conformational changes of the regulatory particle couple ATP hydrolysis to substrate translocation and regulate gating of the core particle, leading to processive degradation. PubMed: 27791164DOI: 10.1073/pnas.1614614113 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.8 Å) |
Structure validation
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