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Open data
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Basic information
| Entry | Database: PDB / ID: 13io | |||||||||||||||||||||
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| Title | MCU-EMRE complex with spermine | |||||||||||||||||||||
Components |
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Keywords | MEMBRANE PROTEIN / mitochondrial calcium uniporter / MCU / EMRE | |||||||||||||||||||||
| Function / homology | Function and homology informationuniporter activity / uniplex complex / positive regulation of mitochondrial calcium ion concentration / Processing of SMDT1 / Mitochondrial calcium ion transport / mitochondrial calcium ion transmembrane transport / mitochondrial calcium ion homeostasis / calcium import into the mitochondrion / channel activator activity / cellular response to calcium ion starvation ...uniporter activity / uniplex complex / positive regulation of mitochondrial calcium ion concentration / Processing of SMDT1 / Mitochondrial calcium ion transport / mitochondrial calcium ion transmembrane transport / mitochondrial calcium ion homeostasis / calcium import into the mitochondrion / channel activator activity / cellular response to calcium ion starvation / positive regulation of neutrophil chemotaxis / positive regulation of mitochondrial fission / protein complex oligomerization / calcium channel complex / Mitochondrial protein degradation / generation of precursor metabolites and energy / calcium-mediated signaling / calcium channel activity / positive regulation of insulin secretion / cell migration / glucose homeostasis / protein-macromolecule adaptor activity / cell population proliferation / mitochondrial inner membrane / mitochondrial matrix / mitochondrion / nucleoplasm / identical protein binding Similarity search - Function | |||||||||||||||||||||
| Biological species | Homo sapiens (human) | |||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.98 Å | |||||||||||||||||||||
Authors | Wang, Q. / Balderas, E. / Rai, N.K. / Cao, E. / Chaudhuri, D. | |||||||||||||||||||||
| Funding support | United States, 3items
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Citation | Journal: To Be PublishedTitle: MCU-EMRE complex with spermine Authors: Wang, Q. / Balderas, E. / Rai, N.K. / Cao, E. / Chaudhuri, D. | |||||||||||||||||||||
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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 | 13io.cif.gz | 217.9 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb13io.ent.gz | 160 KB | Display | PDB format |
| PDBx/mmJSON format | 13io.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/3i/13io ftp://data.pdbj.org/pub/pdb/validation_reports/3i/13io | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 77084 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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| 1 |
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Components
-Protein , 2 types, 8 molecules ABCDEFGH
| #1: Protein | Mass: 5864.078 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: SMDT1, C22orf32, EMRE / Production host: Homo sapiens (human) / References: UniProt: Q9H4I9#2: Protein | Mass: 20502.756 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: MCU, C10orf42, CCDC109A / Production host: Homo sapiens (human) / References: UniProt: Q8NE86 |
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-Non-polymers , 4 types, 11 molecules 






| #3: Chemical | | #4: Chemical | ChemComp-P5S / #5: Chemical | ChemComp-CDL / #6: Chemical | ChemComp-SPM / | |
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-Details
| Has ligand of interest | Y |
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| 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: MCU-EMRE complex with spermine / Type: COMPLEX / Entity ID: #1-#2 / Source: RECOMBINANT |
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| Molecular weight | Experimental value: NO |
| Source (natural) | Organism: Homo sapiens (human) |
| Source (recombinant) | Organism: Homo sapiens (human) |
| Buffer solution | pH: 7.4 |
| 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: 2500 nm / Nominal defocus min: 500 nm |
| Image recording | Electron dose: 45 e/Å2 / Film or detector model: TFS FALCON 4i (4k x 4k) |
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Processing
| EM software |
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||
| 3D reconstruction | Resolution: 2.98 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 84413 / Symmetry type: POINT | ||||||||||||||||
| Atomic model building | Protocol: AB INITIO MODEL | ||||||||||||||||
| Refinement | Cross valid method: NONE |
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About Yorodumi




Homo sapiens (human)
United States, 3items
Citation
PDBj




FIELD EMISSION GUN