|Entry||Database: PDB / ID: 6he4|
|Title||AAA-ATPase ring of PAN-proteasomes|
|Keywords||HYDROLASE / PAN / Proteasome / AAA-ATPase / Archaea|
|Function / homology||AAA+ lid domain / Proteasome-activating nucleotidase PAN / AAA-protein family signature. / Proteasomal ATPase OB C-terminal domain / ATPase family associated with various cellular activities (AAA) / Proteasomal ATPase OB C-terminal domain / P-loop containing nucleoside triphosphate hydrolase / 26S proteasome regulatory subunit P45-like / ATPase, AAA-type, conserved site / ATPase, AAA-type, core ...AAA+ lid domain / Proteasome-activating nucleotidase PAN / AAA-protein family signature. / Proteasomal ATPase OB C-terminal domain / ATPase family associated with various cellular activities (AAA) / Proteasomal ATPase OB C-terminal domain / P-loop containing nucleoside triphosphate hydrolase / 26S proteasome regulatory subunit P45-like / ATPase, AAA-type, conserved site / ATPase, AAA-type, core / AAA+ ATPase domain / proteasome-activating nucleotidase complex / protein unfolding / proteasomal protein catabolic process / ATPase activity / ATP binding / cytoplasm / Proteasome-activating nucleotidase|
Function and homology information
|Specimen source||Archaeoglobus fulgidus (archaea)|
|Method||ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / 4.85 Å resolution|
|Authors||Majumder, P. / Rudack, T. / Beck, F. / Baumeister, W.|
|Citation||Journal: Proc. Natl. Acad. Sci. U.S.A. / Year: 2019|
Title: Cryo-EM structures of the archaeal PAN-proteasome reveal an around-the-ring ATPase cycle.
Authors: Parijat Majumder / Till Rudack / Florian Beck / Radostin Danev / Günter Pfeifer / István Nagy / Wolfgang Baumeister
Abstract: Proteasomes occur in all three domains of life, and are the principal molecular machines for the regulated degradation of intracellular proteins. They play key roles in the maintenance of protein ...Proteasomes occur in all three domains of life, and are the principal molecular machines for the regulated degradation of intracellular proteins. They play key roles in the maintenance of protein homeostasis, and control vital cellular processes. While the eukaryotic 26S proteasome is extensively characterized, its putative evolutionary precursor, the archaeal proteasome, remains poorly understood. The primordial archaeal proteasome consists of a 20S proteolytic core particle (CP), and an AAA-ATPase module. This minimal complex degrades protein unassisted by non-ATPase subunits that are present in a 26S proteasome regulatory particle (RP). Using cryo-EM single-particle analysis, we determined structures of the archaeal CP in complex with the AAA-ATPase PAN (proteasome-activating nucleotidase). Five conformational states were identified, elucidating the functional cycle of PAN, and its interaction with the CP. Coexisting nucleotide states, and correlated intersubunit signaling features, coordinate rotation of the PAN-ATPase staircase, and allosterically regulate N-domain motions and CP gate opening. These findings reveal the structural basis for a sequential around-the-ring ATPase cycle, which is likely conserved in AAA-ATPases.
SummaryFull reportAbout validation report
|Date||Deposition: Aug 20, 2018 / Release: Dec 26, 2018|
|Structure viewer||Molecule: |
Downloads & links
H: Proteasome-activating nucleotidase
I: Proteasome-activating nucleotidase
K: Proteasome-activating nucleotidase
L: Proteasome-activating nucleotidase
M: Proteasome-activating nucleotidase
J: Proteasome-activating nucleotidase
Mass: 29738.418 Da / Num. of mol.: 6
Source: (gene. exp.) Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126) (archaea)
Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126
Gene: pan, AF_1976 / Production host: Escherichia coli (E. coli) / References: UniProt: O28303
Mass: 507.181 Da / Num. of mol.: 4 / Formula: C10H16N5O13P3 / Adenosine triphosphate / Comment: ATP (energy-carrying molecule) *YM
|#4: Chemical|| ChemComp-ADP / |
|Experiment||Method: ELECTRON MICROSCOPY|
|EM experiment||Aggregation state: PARTICLE / Reconstruction method: single particle reconstruction|
|Component||Name: PAN-proteasome / Type: COMPLEX / Entity ID: 1 / Source: RECOMBINANT|
|Molecular weight||Value: 1.25 MDa / Experimental value: NO|
|Source (natural)||Organism: Archaeoglobus fulgidus DSM 4304 (archaea)|
|Source (recombinant)||Organism: Escherichia coli (E. coli)|
|Buffer solution||pH: 7.1|
|Specimen||Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES|
|Vitrification||Cryogen name: ETHANE-PROPANE|
-Electron microscopy imaging
Model: Titan Krios / Image courtesy: FEI Company
|Microscopy||Microscope model: FEI TITAN KRIOS|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM|
|Electron lens||Mode: BRIGHT FIELDBright-field microscopy|
|Image recording||Electron dose: 30 e/Å2 / Detector mode: SUPER-RESOLUTION / Film or detector model: GATAN K2 SUMMIT (4k x 4k)|
|CTF correction||Type: PHASE FLIPPING AND AMPLITUDE CORRECTION|
|Symmetry||Point symmetry: C1|
|3D reconstruction||Resolution: 4.85 Å / Resolution method: FSC 0.143 CUT-OFF / Number of particles: 82207 / Symmetry type: POINT|
|Atomic model building||Ref protocol: FLEXIBLE FIT / Ref space: REAL|
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