|Entry||Database: PDB / ID: 6opc|
|Title||Cdc48 Hexamer in a complex with substrate and Shp1(Ubx Domain)|
|Keywords||MOTOR PROTEIN / Cdc48 / AAA+ ATPase / substrate translocation|
|Function / homology|
Function and homology information
Neutrophil degranulation / Ovarian tumor domain proteases / HSF1 activation / Translesion Synthesis by POLH / SCF complex disassembly in response to cadmium stress / Doa10p ubiquitin ligase complex / RQC complex / Cdc48p-Npl4p-Vms1p AAA ATPase complex / endoplasmic reticulum membrane fusion / nuclear envelope reassembly ...Neutrophil degranulation / Ovarian tumor domain proteases / HSF1 activation / Translesion Synthesis by POLH / SCF complex disassembly in response to cadmium stress / Doa10p ubiquitin ligase complex / RQC complex / Cdc48p-Npl4p-Vms1p AAA ATPase complex / endoplasmic reticulum membrane fusion / nuclear envelope reassembly / cellular protein complex disassembly / ribophagy / stress-induced homeostatically regulated protein degradation pathway / Hrd1p ubiquitin ligase ERAD-L complex / ribosome-associated ubiquitin-dependent protein catabolic process / cytoplasm protein quality control by the ubiquitin-proteasome system / nuclear protein quality control by the ubiquitin-proteasome system / mitochondria-associated ubiquitin-dependent protein catabolic process / sister chromatid biorientation / positive regulation of histone H2B ubiquitination / positive regulation of mitochondrial fusion / ascospore formation / protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway / protein phosphatase regulator activity / mitotic spindle disassembly / piecemeal microautophagy of the nucleus / ER-associated misfolded protein catabolic process / VCP-NPL4-UFD1 AAA ATPase complex / nonfunctional rRNA decay / vesicle-fusing ATPase / retrograde protein transport, ER to cytosol / membrane fusion / mating projection tip / autophagosome maturation / Golgi organization / ATP metabolic process / autophagosome assembly / polyubiquitin modification-dependent protein binding / glycogen metabolic process / ubiquitin-dependent ERAD pathway / negative regulation of telomerase activity / ubiquitin binding / macroautophagy / positive regulation of protein localization to nucleus / proteasome-mediated ubiquitin-dependent protein catabolic process / ATPase activity / endoplasmic reticulum membrane / mitochondrion / ATP binding / identical protein binding / nucleus / cytosol / cytoplasm
UBA-like domain / P-loop containing nucleoside triphosphate hydrolase / ATPase family associated with various cellular activities (AAA) / ATPase, AAA-type, core / AAA ATPase, AAA+ lid domain / NSFL1 cofactor p47, SEP domain superfamily / Ubiquitin-like domain superfamily / CDC48 domain 2-like superfamily / Vps4 oligomerisation, C-terminal / Cell division protein 48 (CDC48), N-terminal domain ...UBA-like domain / P-loop containing nucleoside triphosphate hydrolase / ATPase family associated with various cellular activities (AAA) / ATPase, AAA-type, core / AAA ATPase, AAA+ lid domain / NSFL1 cofactor p47, SEP domain superfamily / Ubiquitin-like domain superfamily / CDC48 domain 2-like superfamily / Vps4 oligomerisation, C-terminal / Cell division protein 48 (CDC48), N-terminal domain / SEP domain / Aspartate decarboxylase-like domain superfamily / AAA ATPase, CDC48 family / CDC48, domain 2 / ATPase, AAA-type, conserved site / UBX domain / CDC48, N-terminal subdomain / UBX domain / AAA+ ATPase domain / UBX domain profile. / AAA-protein family signature. / Cell division protein 48 (CDC48), domain 2 / SEP domain / Vps4 C terminal oligomerisation domain / AAA+ lid domain / SEP domain profile.
Cell division control protein 48 / UBX domain-containing protein 1
|Biological species||Saccharomyces cerevisiae (baker's yeast)|
|Method||ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.7 Å|
|Authors||Cooney, I. / Han, H. / Stewart, M. / Carson, R.H. / Hansen, D. / Price, J.C. / Hill, C.P. / Shen, P.S.|
|Funding support||United States , 1件 |
|Citation||Journal: Science / Year: 2019|
Title: Structure of the Cdc48 segregase in the act of unfolding an authentic substrate.
Authors: Ian Cooney / Han Han / Michael G Stewart / Richard H Carson / Daniel T Hansen / Janet H Iwasa / John C Price / Christopher P Hill / Peter S Shen /
Abstract: The cellular machine Cdc48 functions in multiple biological pathways by segregating its protein substrates from a variety of stable environments such as organelles or multi-subunit complexes. Despite ...The cellular machine Cdc48 functions in multiple biological pathways by segregating its protein substrates from a variety of stable environments such as organelles or multi-subunit complexes. Despite extensive studies, the mechanism of Cdc48 has remained obscure, and its reported structures are inconsistent with models of substrate translocation proposed for other AAA+ ATPases. Here, we report a 3.7 Å resolution structure of Cdc48 in complex with an adaptor protein and a native substrate. Cdc48 engages substrate by adopting a helical configuration of substrate-binding residues that extends through the central pore of both of the ATPase rings. These findings indicate a unified hand-over-hand mechanism of protein translocation by Cdc48 and other AAA+ ATPases.
SummaryFull reportAbout validation report
|Date||Deposition: Apr 24, 2019 / Release: Jul 10, 2019|
|Structure viewer||Molecule: |
Downloads & links
A: Cell division control protein 48
B: Cell division control protein 48
C: Cell division control protein 48
D: Cell division control protein 48
E: Cell division control protein 48
F: Cell division control protein 48
G: Substrate bound to the central pore of the Cdc48 hexamer
Z: UBX domain-containing protein 1
-Protein/peptide , 3 types, 8 molecules A
B C D E F G Z
Mass: 92106.914 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (baker's yeast) / References: UniProt: P25694, vesicle-fusing ATPase
Mass: 1890.321 Da / Num. of mol.: 1 / Details: co-purified with Cdc48 hexamer / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (baker's yeast)
Mass: 47041.105 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (baker's yeast) / References: UniProt: P34223
-Non-polymers , 3 types, 26 molecules
Mass: 427.201 Da / Num. of mol.: 10 / Source method: obtained synthetically / Formula: C10H15N5O10P2 / Adenosine diphosphate / Comment: ADP (energy-carrying molecule) *YM
|Experiment||Method: ELECTRON MICROSCOPY|
|EM experiment||Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction|
|Component||Name: Cdc48-Substrate Complex / Type: COMPLEX / Entity ID: 1, 2, 3 / Source: NATURAL|
|Molecular weight||Units: MEGADALTONS / Experimental value: NO|
|Source (natural)||Organism: Saccharomyces cerevisiae (baker's yeast)|
|Buffer solution||pH: 7.4|
|Specimen||Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES|
|Specimen support||Details: unspecified|
|Vitrification||Cryogen name: ETHANE|
-Electron microscopy imaging
Model: Talos Arctica / Image courtesy: FEI Company
|Microscopy||Model: FEI TALOS ARCTICA|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 200 kV / Illumination mode: FLOOD BEAM|
|Electron lens||Mode: BRIGHT FIELDBright-field microscopy|
|Image recording||Electron dose: 48 e/Å2 / Detector mode: SUPER-RESOLUTION / Film or detector model: GATAN K2 SUMMIT (4k x 4k)|
|CTF correction||Type: PHASE FLIPPING AND AMPLITUDE CORRECTION|
|3D reconstruction||Resolution: 3.7 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 54367 / Symmetry type: POINT|
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