EMDB/PDB/SASBDBから引用されている文献のデータベース

キーワード
構造解析手法	All X線回折 NMR 電子顕微鏡小角散乱中性子線回折線維回折粉末回折赤外分光 EPR FRET 理論モデルハイブリッド
著者・登録者
ジャーナル
IF	>30 >20 >10 >5 all

タイトル	Cryo-EM structures and dynamics of substrate-engaged human 26S proteasome.
ジャーナル・号・ページ	Nature, Vol. 565, Issue 7737, Page 49-55, Year 2019
掲載日	2018年11月12日
著者	Yuanchen Dong / Shuwen Zhang / Zhaolong Wu / Xuemei Li / Wei Li Wang / Yanan Zhu / Svetla Stoilova-McPhie / Ying Lu / Daniel Finley / Youdong Mao /
PubMed 要旨	The proteasome is an ATP-dependent, 2.5-megadalton molecular machine that is responsible for selective protein degradation in eukaryotic cells. Here we present cryo-electron microscopy structures of ...The proteasome is an ATP-dependent, 2.5-megadalton molecular machine that is responsible for selective protein degradation in eukaryotic cells. Here we present cryo-electron microscopy structures of the substrate-engaged human proteasome in seven conformational states at 2.8-3.6 Å resolution, captured during breakdown of a polyubiquitylated protein. These structures illuminate a spatiotemporal continuum of dynamic substrate-proteasome interactions from ubiquitin recognition to substrate translocation, during which ATP hydrolysis sequentially navigates through all six ATPases. There are three principal modes of coordinated hydrolysis, featuring hydrolytic events in two oppositely positioned ATPases, in two adjacent ATPases and in one ATPase at a time. These hydrolytic modes regulate deubiquitylation, initiation of translocation and processive unfolding of substrates, respectively. Hydrolysis of ATP powers a hinge-like motion in each ATPase that regulates its substrate interaction. Synchronization of ATP binding, ADP release and ATP hydrolysis in three adjacent ATPases drives rigid-body rotations of substrate-bound ATPases that are propagated unidirectionally in the ATPase ring and unfold the substrate.
リンク	Nature / PubMed:30479383 / PubMed Central
手法	EM (単粒子)
解像度	2.8 - 3.6 Å
構造データ	EMDB-9215: Cryo-EM structures and dynamics of substrate-engaged human 26S proteasome 手法: EM (単粒子) / 解像度: 2.8 Å 9216 6msb EMDB-9216, PDB-6msb: Cryo-EM structures and dynamics of substrate-engaged human 26S proteasome 手法: EM (単粒子) / 解像度: 3.0 Å 9217 6msd EMDB-9217, PDB-6msd: Cryo-EM structures and dynamics of substrate-engaged human 26S proteasome 手法: EM (単粒子) / 解像度: 3.2 Å 9218 6mse EMDB-9218, PDB-6mse: Cryo-EM structures and dynamics of substrate-engaged human 26S proteasome 手法: EM (単粒子) / 解像度: 3.3 Å 9219 6msg EMDB-9219, PDB-6msg: Cryo-EM structures and dynamics of substrate-engaged human 26S proteasome 手法: EM (単粒子) / 解像度: 3.5 Å 9220 6msh EMDB-9220, PDB-6msh: Cryo-EM structures and dynamics of substrate-engaged human 26S proteasome 手法: EM (単粒子) / 解像度: 3.6 Å 9221 6msj EMDB-9221, PDB-6msj: Cryo-EM structures and dynamics of substrate-engaged human 26S proteasome 手法: EM (単粒子) / 解像度: 3.3 Å 9222 6msk EMDB-9222, PDB-6msk: Cryo-EM structures and dynamics of substrate-engaged human 26S proteasome 手法: EM (単粒子) / 解像度: 3.2 Å EMDB-9223: Cryo-EM structures and dynamics of substrate-engaged human 26S proteasome 手法: EM (単粒子) / 解像度: 3.0 Å EMDB-9224: Cryo-EM structures and dynamics of substrate-engaged human 26S proteasome 手法: EM (単粒子) / 解像度: 3.2 Å EMDB-9225: Cryo-EM structures and dynamics of substrate-engaged human 26S proteasome 手法: EM (単粒子) / 解像度: 3.3 Å EMDB-9226: Cryo-EM structures and dynamics of substrate-engaged human 26S proteasome 手法: EM (単粒子) / 解像度: 3.5 Å EMDB-9227: Cryo-EM structures and dynamics of substrate-engaged human 26S proteasome 手法: EM (単粒子) / 解像度: 3.6 Å EMDB-9228: Cryo-EM structures and dynamics of substrate-engaged human 26S proteasome 手法: EM (単粒子) / 解像度: 3.3 Å EMDB-9229: Cryo-EM structures and dynamics of substrate-engaged human 26S proteasome 手法: EM (単粒子) / 解像度: 3.2 Å
化合物	ChemComp-ZN: Unknown entry ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP / ATP, エネルギー貯蔵分子YM ChemComp-MG: Unknown entry / マグネシウムジカチオン ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP / ADP, エネルギー貯蔵分子YM
由来	homo sapiens (ヒト) saccharomyces cerevisiae rm11-1a (パン酵母)
キーワード	HYDROLASE / Proteosome