Structural mechanism for nucleotide-driven remodeling of the AAA-ATPase unfoldase in the activated human 26S proteasome
The 26S proteasome consists of a core particle that is capped at each side by a regulatory particle. Here the authors present cryo-EM structures of the activated human 26S proteasome holoenzyme in three alternative open-gate states, which provides mechanistic insights into gate opening and dynamic r...
Main Authors: | Yanan Zhu, Wei Li Wang, Daqi Yu, Qi Ouyang, Ying Lu, Youdong Mao |
---|---|
Format: | Article |
Language: | English |
Published: |
Nature Publishing Group
2018-04-01
|
Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/s41467-018-03785-w |
Similar Items
-
Structure of a AAA+ unfoldase in the process of unfolding substrate
by: Zev A Ripstein, et al.
Published: (2017-04-01) -
AAA+ ATPases in Protein Degradation: Structures, Functions and Mechanisms
by: Shuwen Zhang, et al.
Published: (2020-04-01) -
Design framework of the MuA remodeling signal that confers preferential complex disassembly by the AAA+ unfoldase ClpX
by: Ling, Lorraine, Ph. D. Massachusetts Institute of Technology
Published: (2015) -
Deciphering the Roles of Multicomponent Recognition Signals by the AAA+ Unfoldase ClpX
by: Montaño, Sherwin P., et al.
Published: (2017) -
Auto-tethering as a selection mechanism for recognition of multimeric substrates by the AAA+ unfoldase ClpX
by: Abdelhakim, Aliaa H. (Aliaa Hamid)
Published: (2014)