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Open data
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Basic information
| Entry | Database: PDB / ID: 33hm | ||||||||||||
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| Title | Murine RNF213 (Y434A) | ||||||||||||
Components | E3 ubiquitin-protein ligase RNF213 | ||||||||||||
Keywords | SUGAR BINDING PROTEIN / E3 ubiquitin ligase / AAA+ ATPase / CBM20 | ||||||||||||
| Function / homology | Function and homology informationlipid ubiquitination / negative regulation of non-canonical Wnt signaling pathway / xenophagy / lipid droplet formation / sprouting angiogenesis / Transferases; Acyltransferases; Aminoacyltransferases / Antigen processing: Ubiquitination & Proteasome degradation / regulation of lipid metabolic process / protein K63-linked ubiquitination / protein autoubiquitination ...lipid ubiquitination / negative regulation of non-canonical Wnt signaling pathway / xenophagy / lipid droplet formation / sprouting angiogenesis / Transferases; Acyltransferases; Aminoacyltransferases / Antigen processing: Ubiquitination & Proteasome degradation / regulation of lipid metabolic process / protein K63-linked ubiquitination / protein autoubiquitination / lipid droplet / RING-type E3 ubiquitin transferase / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / ubiquitin-protein transferase activity / angiogenesis / ubiquitin protein ligase activity / ubiquitin-dependent protein catabolic process / defense response to bacterium / protein ubiquitination / nucleolus / ATP hydrolysis activity / metal ion binding / cytosol / cytoplasm Similarity search - Function | ||||||||||||
| Biological species | ![]() | ||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.1 Å | ||||||||||||
Authors | Yip, M.C.J. / Naydenova, K. / Randow, F. | ||||||||||||
| Funding support | United Kingdom, European Union, 3items
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Citation | Journal: Nature / Year: 2026Title: Quality control of glycogen through direct ubiquitylation by RNF213. Authors: Matthew C J Yip / Katerina Naydenova / Elsje G Otten / Alexander Heatley / Agnes Moe / Leonie Anton / Lucía de Los Reyes-Ramírez / Helen E Jolin / Frederic Langevin / Michal Wiacek / ...Authors: Matthew C J Yip / Katerina Naydenova / Elsje G Otten / Alexander Heatley / Agnes Moe / Leonie Anton / Lucía de Los Reyes-Ramírez / Helen E Jolin / Frederic Langevin / Michal Wiacek / Catarina Franco / Anne Bertolotti / Wanda Kukulski / Andrew N J McKenzie / Felix Randow / ![]() Abstract: Quality control of biomolecules is vital for organismal health. While DNA repair and protein quality control are well understood, how cells monitor other important biomolecules such as glycogen ...Quality control of biomolecules is vital for organismal health. While DNA repair and protein quality control are well understood, how cells monitor other important biomolecules such as glycogen remains ill-defined. The accumulation of aberrant, poorly branched glycogen into insoluble polyglucosan bodies causes severe disease. Here, we discover autophagy of ubiquitylated aberrant glycogen as a previously unrecognized quality control mechanism safeguarding the brain from polyglucosan buildup. This mechanism depends on the E3 ubiquitin ligase RNF213. Mice lacking ligase activity in RNF213 accumulate polyglucosan in cerebellum, pons, and hippocampus. Using cells engineered to produce polyglucosan, we show that RNF213 selectively ubiquitylates abnormal glycogen. Cryo-EM analysis of RNF213 bound to glycogen-derived maltoheptaose revealed its CBM20 domain binds linear oligosaccharides. Disrupting carbohydrate binding results in gain of E3 ligase activity towards physiological glycogen, indicating the CBM20 domain limits RNF213 activity towards physiological glycogen. Epistasis analysis places RNF213 upstream of LUBAC, suggesting a hierarchical network of multiple E3 ligases surveying glycogen quality. Ubiquitylated polyglucosan recruits the autophagy receptors SQSTM1, TAX1BP1, and optineurin, thereby triggering uptake into autophagosomes. These findings identify RNF213 as a quality control factor preventing polyglucosan accumulation in astrocytes through direct ubiquitylation of polyglucosan, revealing an essential role for non-protein ubiquitylation in glycogen quality control. | ||||||||||||
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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 | 33hm.cif.gz | 925.8 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb33hm.ent.gz | 732.2 KB | Display | PDB format |
| PDBx/mmJSON format | 33hm.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/3h/33hm ftp://data.pdbj.org/pub/pdb/validation_reports/3h/33hm | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 59444MC ![]() 9t8hC ![]() 9t8iC C: citing same article ( M: map data used to model this data |
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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
| #1: Protein | Mass: 589189.500 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: Y434A mutant / Source: (gene. exp.) ![]() Trichoplusia ni (cabbage looper)References: UniProt: E9Q555, RING-type E3 ubiquitin transferase, Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement, Transferases; ...References: UniProt: E9Q555, RING-type E3 ubiquitin transferase, Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement, Transferases; Acyltransferases; Aminoacyltransferases | ||||
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| #2: Chemical | ChemComp-ATP / | ||||
| #3: Chemical | | Has ligand of interest | N | Has protein modification | N | |
-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
| Component | Name: Murine RNF213 (Y434A) / Type: COMPLEX / Entity ID: #1 / Source: RECOMBINANT |
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| Source (natural) | Organism: ![]() |
| Source (recombinant) | Organism: Trichoplusia ni (cabbage looper) |
| Buffer solution | pH: 7.5 |
| 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: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 3000 nm / Nominal defocus min: 1000 nm |
| Image recording | Electron dose: 32.53 e/Å2 / Film or detector model: TFS FALCON 4i (4k x 4k) |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||
| 3D reconstruction | Resolution: 3.1 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 176026 / Symmetry type: POINT |
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About Yorodumi






United Kingdom, European Union, 3items
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PDBj



Trichoplusia ni (cabbage looper)


FIELD EMISSION GUN