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| Title | Substrate-engaged 26 proteasome structures reveal mechanisms for ATP-hydrolysis-driven translocation. |
|---|---|
| Journal, issue, pages | Science, Vol. 362, Issue 6418, Year 2018 |
| Publish date | Nov 30, 2018 |
 Authors | Andres H de la Peña / Ellen A Goodall / Stephanie N Gates / Gabriel C Lander / Andreas Martin /  |
| PubMed Abstract | The 26 proteasome is the primary eukaryotic degradation machine and thus is critically involved in numerous cellular processes. The heterohexameric adenosine triphosphatase (ATPase) motor of the ...The 26 proteasome is the primary eukaryotic degradation machine and thus is critically involved in numerous cellular processes. The heterohexameric adenosine triphosphatase (ATPase) motor of the proteasome unfolds and translocates targeted protein substrates into the open gate of a proteolytic core while a proteasomal deubiquitinase concomitantly removes substrate-attached ubiquitin chains. However, the mechanisms by which ATP hydrolysis drives the conformational changes responsible for these processes have remained elusive. Here we present the cryo-electron microscopy structures of four distinct conformational states of the actively ATP-hydrolyzing, substrate-engaged 26 proteasome. These structures reveal how mechanical substrate translocation accelerates deubiquitination and how ATP-binding, -hydrolysis, and phosphate-release events are coordinated within the AAA+ (ATPases associated with diverse cellular activities) motor to induce conformational changes and propel the substrate through the central pore. |
 External links | Science / PubMed:30309908 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 4.17 - 4.73 Å |
| Structure data | EMDB-9042, PDB-6ef0: EMDB-9043, PDB-6ef1: |
| Chemicals |  ChemComp-ADP:  ChemComp-ATP: |
| Source |
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 Keywords |  MOTOR PROTEIN / 26S Proteasome / ATPase / AAA+ / Protease / Ubiquitin |
