6EF2

Yeast 26S proteasome bound to ubiquitinated substrate (5T motor state)

Summary for 6EF2

• Entry DOI: 10.2210/pdb6ef2/pdb
• Related: 6EF0 6EF1 6EF2 6EF3
• EMDB information: 9042 9043 9044 9045
• Descriptor: Proteasome subunit alpha type-1, 26S proteasome regulatory subunit 8 homolog, 26S proteasome regulatory subunit 6B homolog, ... (16 entities in total)
• Functional Keywords: 26s proteasome, atpase, aaa+, protease, motor protein, ubiquitin
• Biological source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast); More
• Total number of polymer chains: 14
• Total formula weight: 368203.29

Authors

de la Pena, A.H.,Goodall, E.A.,Gates, S.N.,Lander, G.C.,Martin, A. (deposition date: 2018-08-15, release date: 2018-10-17, Last modification date: 2024-03-13)

Primary citation

de la Pena, A.H.,Goodall, E.A.,Gates, S.N.,Lander, G.C.,Martin, A.
Substrate-engaged 26Sproteasome structures reveal mechanisms for ATP-hydrolysis-driven translocation.
Science, 362:-, 2018

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 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.

PubMed: 30309908
DOI: 10.1126/science.aav0725

Experimental method

ELECTRON MICROSCOPY (4.27 Å)