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Open data
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Basic information
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Title | Cryo-EM structure of dodecamer P97 | |||||||||
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![]() | AAA ATPase / CYTOSOLIC PROTEIN | |||||||||
Function / homology | ![]() positive regulation of Lys63-specific deubiquitinase activity / flavin adenine dinucleotide catabolic process / positive regulation of oxidative phosphorylation / VCP-NSFL1C complex / protein-DNA covalent cross-linking repair / endoplasmic reticulum stress-induced pre-emptive quality control / endosome to lysosome transport via multivesicular body sorting pathway / cellular response to arsenite ion / Derlin-1 retrotranslocation complex / BAT3 complex binding ...positive regulation of Lys63-specific deubiquitinase activity / flavin adenine dinucleotide catabolic process / positive regulation of oxidative phosphorylation / VCP-NSFL1C complex / protein-DNA covalent cross-linking repair / endoplasmic reticulum stress-induced pre-emptive quality control / endosome to lysosome transport via multivesicular body sorting pathway / cellular response to arsenite ion / Derlin-1 retrotranslocation complex / BAT3 complex binding / positive regulation of protein K63-linked deubiquitination / deubiquitinase activator activity / aggresome assembly / regulation of protein localization to chromatin / vesicle-fusing ATPase / mitotic spindle disassembly / VCP-NPL4-UFD1 AAA ATPase complex / NADH metabolic process / cellular response to misfolded protein / stress granule disassembly / K48-linked polyubiquitin modification-dependent protein binding / positive regulation of mitochondrial membrane potential / negative regulation of protein localization to chromatin / ubiquitin-modified protein reader activity / retrograde protein transport, ER to cytosol / regulation of aerobic respiration / positive regulation of ATP biosynthetic process / regulation of synapse organization / ATPase complex / ubiquitin-specific protease binding / ubiquitin-like protein ligase binding / MHC class I protein binding / RHOH GTPase cycle / autophagosome maturation / HSF1 activation / polyubiquitin modification-dependent protein binding / proteasomal protein catabolic process / Protein methylation / endoplasmic reticulum to Golgi vesicle-mediated transport / translesion synthesis / interstrand cross-link repair / negative regulation of smoothened signaling pathway / ERAD pathway / ATP metabolic process / endoplasmic reticulum unfolded protein response / Attachment and Entry / viral genome replication / proteasome complex / lipid droplet / Josephin domain DUBs / N-glycan trimming in the ER and Calnexin/Calreticulin cycle / Hh mutants are degraded by ERAD / macroautophagy / Hedgehog ligand biogenesis / Defective CFTR causes cystic fibrosis / Translesion Synthesis by POLH / positive regulation of protein-containing complex assembly / establishment of protein localization / ABC-family proteins mediated transport / ADP binding / autophagy / Aggrephagy / cytoplasmic stress granule / positive regulation of non-canonical NF-kappaB signal transduction / positive regulation of protein catabolic process / activation of cysteine-type endopeptidase activity involved in apoptotic process / KEAP1-NFE2L2 pathway / azurophil granule lumen / double-strand break repair / Ovarian tumor domain proteases / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / positive regulation of canonical Wnt signaling pathway / E3 ubiquitin ligases ubiquitinate target proteins / Neddylation / site of double-strand break / cellular response to heat / ubiquitin-dependent protein catabolic process / regulation of apoptotic process / protein phosphatase binding / proteasome-mediated ubiquitin-dependent protein catabolic process / secretory granule lumen / ficolin-1-rich granule lumen / Attachment and Entry / protein ubiquitination / protein domain specific binding / intracellular membrane-bounded organelle / DNA repair / glutamatergic synapse / lipid binding / ubiquitin protein ligase binding / DNA damage response / Neutrophil degranulation / endoplasmic reticulum membrane / perinuclear region of cytoplasm / endoplasmic reticulum / ATP hydrolysis activity / protein-containing complex / RNA binding / extracellular exosome / extracellular region Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.0 Å | |||||||||
![]() | Liu S / Wang T | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Cryo-EM structure of dodecamer P97 at 2.99 Angstroms resolution Authors: Liu S / Wang T | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 945.1 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 12.7 KB 12.7 KB | Display Display | ![]() |
Images | ![]() | 159.3 KB | ||
Filedesc metadata | ![]() | 5.4 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 546.3 KB | Display | ![]() |
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Full document | ![]() | 545.9 KB | Display | |
Data in XML | ![]() | 8.7 KB | Display | |
Data in CIF | ![]() | 10.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7wubMC M: atomic model generated by this map C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Voxel size | X=Y=Z: 0.83 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
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Sample components
-Entire : dodecamer complex of P97
Entire | Name: dodecamer complex of P97 |
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Components |
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-Supramolecule #1: dodecamer complex of P97
Supramolecule | Name: dodecamer complex of P97 / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#3 |
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Source (natural) | Organism: ![]() |
-Macromolecule #1: Transitional endoplasmic reticulum ATPase
Macromolecule | Name: Transitional endoplasmic reticulum ATPase / type: protein_or_peptide / ID: 1 / Number of copies: 10 / Enantiomer: LEVO / EC number: vesicle-fusing ATPase |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 84.543727 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: NRPNRLIVDE AINEDNSVVS LSQPKMDELQ LFRGDTVLLK GKKRREAVCI VLSDDTCSDE KIRMNRVVRN NLRVRLGDVI SIQPCPDVK YGKRIHVLPI DDTVEGITGN LFEVYLKPYF LEAYRPIRKG DIFLVRGGMR AVEFKVVETD PSPYCIVAPD T VIHCEGEP ...String: NRPNRLIVDE AINEDNSVVS LSQPKMDELQ LFRGDTVLLK GKKRREAVCI VLSDDTCSDE KIRMNRVVRN NLRVRLGDVI SIQPCPDVK YGKRIHVLPI DDTVEGITGN LFEVYLKPYF LEAYRPIRKG DIFLVRGGMR AVEFKVVETD PSPYCIVAPD T VIHCEGEP IKREDEEESL NEVGYDDIGG CRKQLAQIKE MVELPLRHPA LFKAIGVKPP RGILLYGPPG TGKTLIARAV AN ETGAFFF LINGPEIMSK LAGESESNLR KAFEEAEKNA PAIIFIDELD AIAPKREKTH GEVERRIVSQ LLTLMDGLKQ RAH VIVMAA TNRPNSIDPA LRRFGRFDRE VDIGIPDATG RLEILQIHTK NMKLADDVDL EQVANETHGH VGADLAALCS EAAL QAIRK KMDLIDLEDE TIDAEVMNSL AVTMDDFRWA LSQSNPSALR ETVVEVPQVT WEDIGGLEDV KRELQELVQY PVEHP DKFL KFGMTPSKGV LFYGPPGCGK TLLAKAIANE CQANFISIKG PELLTMWFGE SEANVREIFD KARQAAPCVL FFDELD SIA KARGGNIGDG GGAADRVINQ ILTEMDGMST KKNVFIIGAT NRPDIIDPAI LRPGRLDQLI YIPLPDEKSR VAILKAN LR KSPVAKDVDL EFLAKMTNGF SGADLTEICQ RACKLAIRES IESEIRRERE RQTNPSAMEV EEDDPVPEIR RDHFEEAM R FARRSVSDND IRKYEMFAQT LQQSRGFGSF RFPS UniProtKB: Transitional endoplasmic reticulum ATPase |
-Macromolecule #2: Transitional endoplasmic reticulum ATPase
Macromolecule | Name: Transitional endoplasmic reticulum ATPase / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO / EC number: vesicle-fusing ATPase |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 64.048098 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: EVGYDDIGGC RKQLAQIKEM VELPLRHPAL FKAIGVKPPR GILLYGPPGT GKTLIARAVA NETGAFFFLI NGPEIMSKLA GESESNLRK AFEEAEKNAP AIIFIDELDA IAPKREKTHG EVERRIVSQL LTLMDGLKQR AHVIVMAATN RPNSIDPALR R FGRFDREV ...String: EVGYDDIGGC RKQLAQIKEM VELPLRHPAL FKAIGVKPPR GILLYGPPGT GKTLIARAVA NETGAFFFLI NGPEIMSKLA GESESNLRK AFEEAEKNAP AIIFIDELDA IAPKREKTHG EVERRIVSQL LTLMDGLKQR AHVIVMAATN RPNSIDPALR R FGRFDREV DIGIPDATGR LEILQIHTKN MKLADDVDLE QVANETHGHV GADLAALCSE AALQAIRKKM DLIDLEDETI DA EVMNSLA VTMDDFRWAL SQSNPSALRE TVVEVPQVTW EDIGGLEDVK RELQELVQYP VEHPDKFLKF GMTPSKGVLF YGP PGCGKT LLAKAIANEC QANFISIKGP ELLTMWFGES EANVREIFDK ARQAAPCVLF FDELDSIAKA RGGNIGDGGG AADR VINQI LTEMDGMSTK KNVFIIGATN RPDIIDPAIL RPGRLDQLIY IPLPDEKSRV AILKANLRKS PVAKDVDLEF LAKMT NGFS GADLTEICQR ACKLAIRESI ESEIRRERQT QTNPSAMEVE EDDPVPEIRR DHFEEAMRFA RRSVSDNDIR KYEMFA QTL QQSRGFGSFR FPS UniProtKB: Transitional endoplasmic reticulum ATPase |
-Macromolecule #3: Transitional endoplasmic reticulum ATPase
Macromolecule | Name: Transitional endoplasmic reticulum ATPase / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO / EC number: vesicle-fusing ATPase |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 64.105184 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: EVGYDDIGGC RKQLAQIKEM VELPLRHPAL FKAIGVKPPR GILLYGPPGT GKTLIARAVA NETGAFFFLI NGPEIMSKLA GESESNLRK AFEEAEKNAP AIIFIDELDA IAPKREKTHG EVERRIVSQL LTLMDGLKQR AHVIVMAATN RPNSIDPALR R FGRFDREV ...String: EVGYDDIGGC RKQLAQIKEM VELPLRHPAL FKAIGVKPPR GILLYGPPGT GKTLIARAVA NETGAFFFLI NGPEIMSKLA GESESNLRK AFEEAEKNAP AIIFIDELDA IAPKREKTHG EVERRIVSQL LTLMDGLKQR AHVIVMAATN RPNSIDPALR R FGRFDREV DIGIPDATGR LEILQIHTKN MKLADDVDLE QVANETHGHV GADLAALCSE AALQAIRKKM DLIDLEDETI DA EVMNSLA VTMDDFRWAL SQSNPSALRE TVVEVPQVTW EDIGGLEDVK RELQELVQYP VEHPDKFLKF GMTPSKGVLF YGP PGCGKT LLAKAIANEC QANFISIKGP ELLTMWFGES EANVREIFDK ARQAAPCVLF FDELDSIAKA RGGNIGDGGG AADR VINQI LTEMDGMSTK KNVFIIGATN RPDIIDPAIL RPGRLDQLIY IPLPDEKSRV AILKANLRKS PVAKDVDLEF LAKMT NGFS GADLTEICQR ACKLAIRESI ESEIRRERER QTNPSAMEVE EDDPVPEIRR DHFEEAMRFA RRSVSDNDIR KYEMFA QTL QQSRGFGSFR FPS UniProtKB: Transitional endoplasmic reticulum ATPase |
-Macromolecule #4: ADENOSINE-5'-DIPHOSPHATE
Macromolecule | Name: ADENOSINE-5'-DIPHOSPHATE / type: ligand / ID: 4 / Number of copies: 12 / Formula: ADP |
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Molecular weight | Theoretical: 427.201 Da |
Chemical component information | ![]() ChemComp-ADP: |
-Macromolecule #5: 3-[3-cyclopentylsulfanyl-5-[[3-methyl-4-(4-methylsulfonylphenyl)p...
Macromolecule | Name: 3-[3-cyclopentylsulfanyl-5-[[3-methyl-4-(4-methylsulfonylphenyl)phenoxy]methyl]-1,2,4-triazol-4-yl]pyridine type: ligand / ID: 5 / Number of copies: 12 / Formula: Y6Y |
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Molecular weight | Theoretical: 520.666 Da |
Chemical component information | ![]() ChemComp-Y6Y: |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | 3D array |
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Sample preparation
Buffer | pH: 7.4 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K2 QUANTUM (4k x 4k) / Average electron dose: 50.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELD / Nominal defocus max: 3.0 µm / Nominal defocus min: 1.2 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
Startup model | Type of model: OTHER |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 3.0 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 157000 |
Initial angle assignment | Type: OTHER |
Final angle assignment | Type: OTHER |