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SA-like and SD-like states of human 26S Proteasome with non-cleavable M1-linked hexaubiquitin (dataset 2)

ABSTRACT:

SUBMITTER: Kylie J Walters

PROVIDER: EMPIAR-10402 | biostudies-other |

REPOSITORIES: biostudies-other

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Cryo-EM Reveals Unanchored M1-Ubiquitin Chain Binding at hRpn11 of the 26S Proteasome.

Chen Xiang X Dorris Zachary Z Shi Dan D Huang Rick K RK Khant Htet H Fox Tara T de Val Natalia N Williams Dewight D Zhang Ping P Walters Kylie J KJ

Structure (London, England : 1993) 20200811 11

The 26S proteasome is specialized for regulated protein degradation and formed by a dynamic regulatory particle (RP) that caps a hollow cylindrical core particle (CP) where substrates are proteolyzed. Its diverse substrates unify as proteasome targets by ubiquitination. We used cryogenic electron microscopy (cryo-EM) to study how human 26S proteasome interacts with M1-linked hexaubiquitin (M1-Ub<sub>6</sub>) unanchored to a substrate and E3 ubiquitin ligase E6AP/UBE3A. Proteasome structures are ...[more]

PMID: 32783951

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