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dc.contributor.authorChen, Shuobing
dc.contributor.authorWu, Jiayi
dc.contributor.authorLu, Ying
dc.contributor.authorMa, Yong-Bei
dc.contributor.authorLee, Byung-Hoon
dc.contributor.authorYu, Zhou
dc.contributor.authorOuyang, Qi
dc.contributor.authorFinley, Daniel
dc.contributor.authorKirschner, Marc
dc.contributor.authorMao, Youdong
dc.date.accessioned2019-10-05T09:46:53Z
dc.date.issued2016
dc.identifier.citationChen, Shuobing, Jiayi Wu, Ying Lu, Yong-Bei Ma, Byung-Hoon Lee, Zhou Yu, Qi Ouyang, Daniel J. Finley, Marc W. Kirschner, and Youdong Mao. 2016. “Structural Basis for Dynamic Regulation of the Human 26S Proteasome.” Proceedings of the National Academy of Sciences 113 (46): 12991–96. https://doi.org/10.1073/pnas.1614614113.
dc.identifier.issn0027-8424
dc.identifier.issn0744-2831
dc.identifier.issn1091-6490
dc.identifier.urihttp://nrs.harvard.edu/urn-3:HUL.InstRepos:41483167*
dc.description.abstractThe 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.
dc.language.isoen_US
dc.publisherNational Academy of Sciences
dash.licenseLAA
dc.titleStructural basis for dynamic regulation of the human 26S proteasome
dc.typeJournal Article
dc.description.versionVersion of Record
dc.relation.journalProceedings of the National Academy of Sciences of the United States of America
dash.depositing.authorFinley, Daniel::55733c495443e58aeebdb3090cda00e5::600
dc.date.available2019-10-05T09:46:53Z
dash.workflow.comments1Science Serial ID 91416
dc.identifier.doi10.1073/pnas.1614614113
dash.source.volume113;46
dash.source.page12991


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