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-Structure paper
タイトル | An atomic structure of the human 26S proteasome. |
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ジャーナル・号・ページ | Nat Struct Mol Biol, Vol. 23, Issue 9, Page 778-785, Year 2016 |
掲載日 | 2016年7月18日 |
![]() | Xiuliang Huang / Bai Luan / Jianping Wu / Yigong Shi / ![]() |
PubMed 要旨 | We report the cryo-EM structure of the human 26S proteasome at an average resolution of 3.5 Å, allowing atomic modeling of 28 subunits in the core particle (CP) and 18 subunits in the regulatory ...We report the cryo-EM structure of the human 26S proteasome at an average resolution of 3.5 Å, allowing atomic modeling of 28 subunits in the core particle (CP) and 18 subunits in the regulatory particle (RP). The C-terminal residues of Rpt3 and Rpt5 subunits in the RP can be seen inserted into surface pockets formed between adjacent α subunits in the CP. Each of the six Rpt subunits contains a bound nucleotide, and the central gate of the CP α-ring is closed despite RP association. The six pore 1 loops in the Rpt ring are arranged similarly to a spiral staircase along the axial channel of substrate transport, which is constricted by the pore 2 loops. We also determined the cryo-EM structure of the human proteasome bound to the deubiquitinating enzyme USP14 at 4.35-Å resolution. Together, our structures provide a framework for mechanistic understanding of eukaryotic proteasome function. |
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手法 | EM (単粒子) |
解像度 | 3.5 - 4.6 Å |
構造データ | ![]() EMDB-9507: ![]() EMDB-9508: ![]() EMDB-9509: ![]() EMDB-9510: |
化合物 | ![]() ChemComp-ADP: |
由来 |
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![]() | HYDROLASE / protein complex / human proteasome |