Cryo-EM structures and dynamics of substrate-engaged human 26S proteasome

• Published in: Nature (London) Vol. 565; no. 7737; pp. 49 - 55
• Main Authors: Dong, Yuanchen, Zhang, Shuwen, Wu, Zhaolong, Li, Xuemei, Wang, Wei Li, Zhu, Yanan, Stoilova-McPhie, Svetla, Lu, Ying, Finley, Daniel, Mao, Youdong
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 01.01.2019; Nature Publishing Group
• Subjects: 101/28; 631/45/468; 631/535/1258/1259; 631/80/474/2085; 82/83; Adenosine diphosphate; Adenosine triphosphatase; Adenosine Triphosphatases - metabolism; Adenosine Triphosphate - metabolism; Allosteric Regulation; ATP; ATPases; Automation; Binding sites; Biodegradation; Cell cycle; Cryoelectron Microscopy; Electron microscopy; Holoenzymes - chemistry; Holoenzymes - metabolism; Holoenzymes - ultrastructure; Humanities and Social Sciences; Humans; Hydrolysis; Microscopy; Models, Molecular; Molecular machines; multidisciplinary; Proteasome 26S; Proteasome Endopeptidase Complex - chemistry; Proteasome Endopeptidase Complex - metabolism; Proteasome Endopeptidase Complex - ultrastructure; Protein Conformation; Protein research; Protein Structure, Quaternary; Protein Unfolding; Proteins; Proteolysis; Science; Science (multidisciplinary); Substrate Specificity; Substrates; Synchronism; Synchronization; Translocation; Ubiquitin; Ubiquitin-proteasome system; Ubiquitination

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, captur...