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-Structure paper
タイトル | Cryo-EM Reveals Unanchored M1-Ubiquitin Chain Binding at hRpn11 of the 26S Proteasome. |
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ジャーナル・号・ページ | Structure, Vol. 28, Issue 11, Page 1206-11217.e4, Year 2020 |
掲載日 | 2020年11月3日 |
![]() | Xiang Chen / Zachary Dorris / Dan Shi / Rick K Huang / Htet Khant / Tara Fox / Natalia de Val / Dewight Williams / Ping Zhang / Kylie J Walters / ![]() |
PubMed 要旨 | 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. ...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) unanchored to a substrate and E3 ubiquitin ligase E6AP/UBE3A. Proteasome structures are available with model substrates extending through the RP ATPase ring and substrate-conjugated K63-linked ubiquitin chains present at inhibited deubiquitinating enzyme hRpn11 and the nearby ATPase hRpt4/hRpt5 coiled coil. In this study, we find M1-Ub at the hRpn11 site despite the absence of conjugated substrate, indicating that ubiquitin binding at this location does not require substrate interaction with the RP. Moreover, unanchored M1-Ub binds to this hRpn11 site of the proteasome with the CP gating residues in both the closed and opened conformational states. |
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手法 | EM (単粒子) |
解像度 | 4.1 - 6.75 Å |
構造データ | EMDB-21691, PDB-6wjd: EMDB-21696, PDB-6wjn: ![]() EMDB-21697: ![]() EMDB-21698: ![]() EMDB-21699: ![]() EMDB-21700: ![]() EMDB-21704: |
化合物 | ![]() ChemComp-ZN: ![]() ChemComp-AGS: ![]() ChemComp-MG: ![]() ChemComp-ADP: |
由来 |
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![]() | HYDROLASE/PROTEIN BINDING / 26S protease / ubiquitin / complex / subunit / HYDROLASE-PROTEIN BINDING complex |