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	Structural mechanism for nucleotide-driven remodeling of the AAA-ATPase unfoldase in the activated human 26S proteasome.
Journal, issue, pages	Nat Commun, Vol. 9, Issue 1, Page 1360, Year 2018
Publish date	Apr 10, 2018
Authors	Yanan Zhu / Wei Li Wang / Daqi Yu / Qi Ouyang / Ying Lu / Youdong Mao /
PubMed Abstract	The proteasome is a sophisticated ATP-dependent molecular machine responsible for protein degradation in all known eukaryotic cells. It remains elusive how conformational changes of the AAA-ATPase ...The proteasome is a sophisticated ATP-dependent molecular machine responsible for protein degradation in all known eukaryotic cells. It remains elusive how conformational changes of the AAA-ATPase unfoldase in the regulatory particle (RP) control the gating of the substrate-translocation channel leading to the proteolytic chamber of the core particle (CP). Here we report three alternative states of the ATP-γ-S-bound human proteasome, in which the CP gates are asymmetrically open, visualized by cryo-EM at near-atomic resolutions. At least four nucleotides are bound to the AAA-ATPase ring in these open-gate states. Variation in nucleotide binding gives rise to an axial movement of the pore loops narrowing the substrate-translation channel, which exhibit remarkable structural transitions between the spiral-staircase and saddle-shaped-circle topologies. Gate opening in the CP is thus regulated by nucleotide-driven conformational changes of the AAA-ATPase unfoldase. These findings demonstrate an elegant mechanism of allosteric coordination among sub-machines within the human proteasome holoenzyme.
External links	Nat Commun / PubMed:29636472 / PubMed Central
Methods	EM (single particle)
Resolution	3.5 - 7.0 Å
Structure data	8662 5vfo EMDB-8662, PDB-5vfo: Nucleotide-driven Triple-state Remodeling of the AAA-ATPase Channel in the Activated Human 26S Proteasome Method: EM (single particle) / Resolution: 3.5 Å 8663 5vfp EMDB-8663, PDB-5vfp: Nucleotide-driven Triple-state Remodeling of the AAA-ATPase Channel in the Activated Human 26S Proteasome Method: EM (single particle) / Resolution: 4.2 Å 8664 5vfq EMDB-8664, PDB-5vfq: Nucleotide-driven Triple-state Remodeling of the AAA-ATPase Channel in the Activated Human 26S Proteasome Method: EM (single particle) / Resolution: 4.2 Å 8665 5vfr EMDB-8665, PDB-5vfr: Nucleotide-driven Triple-state Remodeling of the AAA-ATPase Channel in the Activated Human 26S Proteasome Method: EM (single particle) / Resolution: 4.9 Å 8666 5vfs EMDB-8666, PDB-5vfs: Nucleotide-Driven Triple-State Remodeling of the AAA-ATPase Channel in the Activated Human 26S Proteasome Method: EM (single particle) / Resolution: 3.6 Å 8667 5vft EMDB-8667, PDB-5vft: Nucleotide-driven Triple-state Remodeling of the AAA-ATPase Channel in the Activated Human 26S Proteasome Method: EM (single particle) / Resolution: 7.0 Å 8668 5vfu EMDB-8668, PDB-5vfu: Nucleotide-driven Triple-state Remodeling of the AAA-ATPase Channel in the Activated Human 26S Proteasome Method: EM (single particle) / Resolution: 5.8 Å
Chemicals	ChemComp-ZN: Unknown entry ChemComp-AGS: PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER / ATP-gamma-S, energy-carrying molecule analogue*YM
Source	homo sapiens (human)
Keywords	HYDROLASE / 26S proteasome / ATP-dependent protease / AAA-ATPase / peptide-unfolding channel / 20S core particle