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Yorodumi- PDB-9qo2: Dissociation-state-1 of 9-subunit CSN and SCF (SKP1-SKP2-CKS1) complex -
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Open data
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Basic information
| Entry | Database: PDB / ID: 9qo2 | ||||||||||||||||||||||||
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| Title | Dissociation-state-1 of 9-subunit CSN and SCF (SKP1-SKP2-CKS1) complex | ||||||||||||||||||||||||
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Keywords | LIGASE / E3 ligases / COP9 signalosome | ||||||||||||||||||||||||
| Function / homology | Function and homology informationnegative regulation of protein localization to nucleolus / positive regulation of protein polyubiquitination / COP9 signalosome assembly / trophectodermal cell proliferation / macrophage migration inhibitory factor binding / regulation of IRE1-mediated unfolded protein response / Parkin-FBXW7-Cul1 ubiquitin ligase complex / exosomal secretion / GTPase inhibitor activity / F-box domain binding ...negative regulation of protein localization to nucleolus / positive regulation of protein polyubiquitination / COP9 signalosome assembly / trophectodermal cell proliferation / macrophage migration inhibitory factor binding / regulation of IRE1-mediated unfolded protein response / Parkin-FBXW7-Cul1 ubiquitin ligase complex / exosomal secretion / GTPase inhibitor activity / F-box domain binding / cellular response to cell-matrix adhesion / deNEDDylase activity / Aberrant regulation of mitotic exit in cancer due to RB1 defects / protein deneddylation / regulation of protein neddylation / PcG protein complex / activation of NF-kappaB-inducing kinase activity / eukaryotic translation initiation factor 3 complex / negative regulation of beige fat cell differentiation / cullin-RING-type E3 NEDD8 transferase / NEDD8 transferase activity / COP9 signalosome / positive regulation of ubiquitin protein ligase activity / cullin-RING ubiquitin ligase complex / Cul7-RING ubiquitin ligase complex / maintenance of protein location in nucleus / cellular response to chemical stress / Loss of Function of FBXW7 in Cancer and NOTCH1 Signaling / protein K27-linked ubiquitination / cyclin-dependent protein serine/threonine kinase activator activity / positive regulation of protein autoubiquitination / RNA polymerase II transcription initiation surveillance / negative regulation of protein neddylation / protein neddylation / NEDD8 ligase activity / Hydrolases; Acting on peptide bonds (peptidases) / RHOBTB1 GTPase cycle / metal-dependent deubiquitinase activity / VCB complex / negative regulation of response to oxidative stress / regulation of JNK cascade / regulation of DNA damage response, signal transduction by p53 class mediator / Cul5-RING ubiquitin ligase complex / inner cell mass cell proliferation / ubiquitin-ubiquitin ligase activity / SCF ubiquitin ligase complex / ubiquitin-dependent protein catabolic process via the C-end degron rule pathway / Cul2-RING ubiquitin ligase complex / negative regulation of type I interferon production / SCF-dependent proteasomal ubiquitin-dependent protein catabolic process / positive regulation of intracellular estrogen receptor signaling pathway / Cul3-RING ubiquitin ligase complex / negative regulation of mitophagy / Cul4A-RING E3 ubiquitin ligase complex / Cul4-RING E3 ubiquitin ligase complex / Prolactin receptor signaling / Cul4B-RING E3 ubiquitin ligase complex / ubiquitin ligase complex scaffold activity / response to light stimulus / cullin family protein binding / skeletal muscle cell differentiation / protein K63-linked ubiquitination / protein monoubiquitination / site of DNA damage / : / ubiquitin-like ligase-substrate adaptor activity / protein K48-linked ubiquitination / cyclin-dependent protein kinase holoenzyme complex / positive regulation of double-strand break repair via homologous recombination / : / signal transduction in response to DNA damage / Nuclear events stimulated by ALK signaling in cancer / JNK cascade / transcription-coupled nucleotide-excision repair / translation initiation factor activity / positive regulation of TORC1 signaling / regulation of cellular response to insulin stimulus / positive regulation of smooth muscle cell proliferation / negative regulation of insulin receptor signaling pathway / intrinsic apoptotic signaling pathway / post-translational protein modification / regulation of mitotic cell cycle / molecular function activator activity / T cell activation / negative regulation of canonical NF-kappaB signal transduction / ubiquitin binding / animal organ morphogenesis / Regulation of BACH1 activity / MAP3K8 (TPL2)-dependent MAPK1/3 activation / Degradation of CRY and PER proteins / SCF-beta-TrCP mediated degradation of Emi1 / NIK-->noncanonical NF-kB signaling / cellular response to amino acid stimulus / Vpu mediated degradation of CD4 / Degradation of DVL / Dectin-1 mediated noncanonical NF-kB signaling / Activation of NF-kappaB in B cells / G1/S transition of mitotic cell cycle / Degradation of GLI1 by the proteasome / Iron uptake and transport Similarity search - Function | ||||||||||||||||||||||||
| Biological species | Homo sapiens (human) | ||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.8 Å | ||||||||||||||||||||||||
Authors | Ding, S. / Clapperton, J.A. / Maeots, M.E. / Enchev, R.I. | ||||||||||||||||||||||||
| Funding support | United Kingdom, 1items
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Citation | Journal: Nat Commun / Year: 2026Title: Structural basis of CSN-mediated SCF deneddylation. Authors: Shan Ding / Julie A Clapperton / Märt-Erik Mäeots / Simone Kunzelmann / Mohammed Shaaban / Radoslav I Enchev / ![]() Abstract: Cullin-RING ligases (CRLs) are the largest family of E3 ligases, with ubiquitination activity dynamically regulated by neddylation and deneddylation by the COP9 signalosome (CSN). CSN-mediated ...Cullin-RING ligases (CRLs) are the largest family of E3 ligases, with ubiquitination activity dynamically regulated by neddylation and deneddylation by the COP9 signalosome (CSN). CSN-mediated deneddylation not only deactivates CRLs but also enables substrate receptor exchange. Although CSN is a promising drug target, the structural basis underlying its catalytic mechanism remains unclear. Here, we use cryo-electron microscopy (cryo-EM) to uncover distinct functional states of CSN-CRL (SCF) complexes, capturing key intermediates of the deneddylation cycle. We visualise an autoinhibited docking state and a catalytic intermediate in which CSN5 Ins-1 loop, RBX1 RING and neddylated Cullin WHB domains are repositioned for isopeptide cleavage. We further resolve four dissociation intermediates that define the stepwise release of CSN from its product, with RBX1 RING stabilising key interactions. Additionally, our structures locate CSNAP within a CSN3-CSN8 groove. Together, our study provides a mechanistic model for CSN function and informs the rational design of CSN-targeted therapeutics. | ||||||||||||||||||||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 9qo2.cif.gz | 619.4 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb9qo2.ent.gz | 485.3 KB | Display | PDB format |
| PDBx/mmJSON format | 9qo2.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/qo/9qo2 ftp://data.pdbj.org/pub/pdb/validation_reports/qo/9qo2 | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 53254MC ![]() 9qo0C ![]() 9qo1C ![]() 9qo3C ![]() 9qo4C ![]() 9qo5C ![]() 9qo6C M: map data used to model this data C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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Components
-COP9 signalosome complex subunit ... , 9 types, 9 molecules BCDEFGHPA
| #1: Protein | Mass: 51664.570 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: COPS2, CSN2, TRIP15 / Production host: ![]() |
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| #2: Protein | Mass: 47924.008 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: COPS3, CSN3 / Production host: ![]() |
| #3: Protein | Mass: 46322.688 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: COPS4, CSN4 / Production host: ![]() |
| #4: Protein | Mass: 37621.742 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: COPS5, CSN5, JAB1 / Production host: ![]() References: UniProt: Q92905, Hydrolases; Acting on peptide bonds (peptidases) |
| #5: Protein | Mass: 36203.398 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: COPS6, CSN6, HVIP / Production host: ![]() |
| #6: Protein | Mass: 29656.928 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: COPS7B, CSN7B / Production host: ![]() |
| #7: Protein | Mass: 23245.543 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: COPS8, CSN8 / Production host: ![]() |
| #13: Protein | Mass: 6213.689 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: COPS9, MYEOV2 / Production host: ![]() |
| #14: Protein | Mass: 55606.496 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: GPS1, COPS1, CSN1 / Production host: ![]() |
-Protein , 3 types, 3 molecules IJN
| #8: Protein | Mass: 89800.367 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: CUL1 / Production host: ![]() |
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| #9: Protein | Mass: 12289.977 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: RBX1, RNF75, ROC1 / Production host: ![]() References: UniProt: P62877, RING-type E3 ubiquitin transferase, cullin-RING-type E3 NEDD8 transferase |
| #12: Protein | Mass: 9679.211 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: CKS1B, CKS1, PNAS-143, PNAS-16 / Production host: ![]() |
-S-phase kinase-associated protein ... , 2 types, 2 molecules LM
| #10: Protein | Mass: 18679.965 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: SKP1, EMC19, OCP2, SKP1A, TCEB1L / Production host: ![]() |
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| #11: Protein | Mass: 47817.785 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: SKP2, FBXL1 / Production host: ![]() |
-Non-polymers , 2 types, 4 molecules 


| #15: Chemical | ChemComp-IHP / |
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| #16: Chemical |
-Details
| Has ligand of interest | Y |
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| Has protein modification | Y |
-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
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| EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
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| Buffer solution | pH: 7.5 / Details: 15 mM Hepes pH 7.5, 120 mM NaCl, 0.5 mM DTT | ||||||||||||||||||||||||||||||||||||
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||||||||||||||||||||||
| Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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| Microscopy | Model: TFS KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: SPOT SCAN |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 5000 nm / Nominal defocus min: 500 nm |
| Image recording | Electron dose: 47 e/Å2 / Film or detector model: FEI FALCON III (4k x 4k) |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 3.8 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 1015152 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refinement | Highest resolution: 3.8 Å Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS) | ||||||||||||||||||||||||
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About Yorodumi



Homo sapiens (human)
United Kingdom, 1items
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FIELD EMISSION GUN