Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Cryo-EM structures and dynamics of substrate-engaged human 26S proteasome.
Journal, issue, pages	Nature, Vol. 565, Issue 7737, Page 49-55, Year 2019
Publish date	Nov 12, 2018
Authors	Yuanchen Dong / Shuwen Zhang / Zhaolong Wu / Xuemei Li / Wei Li Wang / Yanan Zhu / Svetla Stoilova-McPhie / Ying Lu / Daniel Finley / Youdong Mao /
PubMed Abstract	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.
External links	Nature / PubMed:30479383 / PubMed Central
Methods	EM (single particle)
Resolution	2.8 - 3.6 Å
Structure data	EMDB-9215: Cryo-EM structures and dynamics of substrate-engaged human 26S proteasome Method: EM (single particle) / Resolution: 2.8 Å 9216 6msb EMDB-9216, PDB-6msb: Cryo-EM structures and dynamics of substrate-engaged human 26S proteasome Method: EM (single particle) / Resolution: 3.0 Å 9217 6msd EMDB-9217, PDB-6msd: Cryo-EM structures and dynamics of substrate-engaged human 26S proteasome Method: EM (single particle) / Resolution: 3.2 Å 9218 6mse EMDB-9218, PDB-6mse: Cryo-EM structures and dynamics of substrate-engaged human 26S proteasome Method: EM (single particle) / Resolution: 3.3 Å 9219 6msg EMDB-9219, PDB-6msg: Cryo-EM structures and dynamics of substrate-engaged human 26S proteasome Method: EM (single particle) / Resolution: 3.5 Å 9220 6msh EMDB-9220, PDB-6msh: Cryo-EM structures and dynamics of substrate-engaged human 26S proteasome Method: EM (single particle) / Resolution: 3.6 Å 9221 6msj EMDB-9221, PDB-6msj: Cryo-EM structures and dynamics of substrate-engaged human 26S proteasome Method: EM (single particle) / Resolution: 3.3 Å 9222 6msk EMDB-9222, PDB-6msk: Cryo-EM structures and dynamics of substrate-engaged human 26S proteasome Method: EM (single particle) / Resolution: 3.2 Å EMDB-9223: Cryo-EM structures and dynamics of substrate-engaged human 26S proteasome Method: EM (single particle) / Resolution: 3.0 Å EMDB-9224: Cryo-EM structures and dynamics of substrate-engaged human 26S proteasome Method: EM (single particle) / Resolution: 3.2 Å EMDB-9225: Cryo-EM structures and dynamics of substrate-engaged human 26S proteasome Method: EM (single particle) / Resolution: 3.3 Å EMDB-9226: Cryo-EM structures and dynamics of substrate-engaged human 26S proteasome Method: EM (single particle) / Resolution: 3.5 Å EMDB-9227: Cryo-EM structures and dynamics of substrate-engaged human 26S proteasome Method: EM (single particle) / Resolution: 3.6 Å EMDB-9228: Cryo-EM structures and dynamics of substrate-engaged human 26S proteasome Method: EM (single particle) / Resolution: 3.3 Å EMDB-9229: Cryo-EM structures and dynamics of substrate-engaged human 26S proteasome Method: EM (single particle) / Resolution: 3.2 Å
Chemicals	ChemComp-ZN: Unknown entry ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying moleculeYM ChemComp-MG: Unknown entry ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying moleculeYM
Source	homo sapiens (human) saccharomyces cerevisiae rm11-1a (yeast)
Keywords	HYDROLASE / Proteosome