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Open data
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Basic information
| Entry | Database: PDB / ID: 6xjv | ||||||
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| Title | MCU holocomplex in High-calcium state | ||||||
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Keywords | TRANSPORT PROTEIN / ion channel | ||||||
| Function / homology | Function and homology informationmitochondrial crista junction / negative regulation of mitochondrial calcium ion concentration / regulation of cellular hyperosmotic salinity response / positive regulation of cristae formation / uniporter activity / mitochondrial calcium ion transmembrane transport / uniplex complex / Processing of SMDT1 / positive regulation of mitochondrial calcium ion concentration / Mitochondrial calcium ion transport ...mitochondrial crista junction / negative regulation of mitochondrial calcium ion concentration / regulation of cellular hyperosmotic salinity response / positive regulation of cristae formation / uniporter activity / mitochondrial calcium ion transmembrane transport / uniplex complex / Processing of SMDT1 / positive regulation of mitochondrial calcium ion concentration / Mitochondrial calcium ion transport / mitochondrial calcium ion homeostasis / calcium import into the mitochondrion / calcium ion sensor activity / channel activator activity / cellular response to calcium ion starvation / calcium ion import / positive regulation of neutrophil chemotaxis / positive regulation of mitochondrial fission / protein complex oligomerization / calcium channel inhibitor activity / calcium channel complex / Mitochondrial protein degradation / cellular response to calcium ion / calcium channel regulator activity / calcium-mediated signaling / defense response / positive regulation of insulin secretion / protein homooligomerization / mitochondrial intermembrane space / mitochondrial membrane / calcium channel activity / glucose homeostasis / protein-macromolecule adaptor activity / mitochondrial inner membrane / mitochondrial matrix / protein heterodimerization activity / calcium ion binding / mitochondrion / nucleoplasm / identical protein binding Similarity search - Function | ||||||
| Biological species | Homo sapiens (human) | ||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4.17 Å | ||||||
Authors | Wang, Y. / Jiang, Y. | ||||||
| Funding support | United States, 1items
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Citation | Journal: Elife / Year: 2020Title: Structural insights into the Ca-dependent gating of the human mitochondrial calcium uniporter. Authors: Yan Wang / Yan Han / Ji She / Nam X Nguyen / Vamsi K Mootha / Xiao-Chen Bai / Youxing Jiang / ![]() Abstract: Mitochondrial Ca uptake is mediated by an inner mitochondrial membrane protein called the mitochondrial calcium uniporter. In humans, the uniporter functions as a holocomplex consisting of MCU, EMRE, ...Mitochondrial Ca uptake is mediated by an inner mitochondrial membrane protein called the mitochondrial calcium uniporter. In humans, the uniporter functions as a holocomplex consisting of MCU, EMRE, MICU1 and MICU2, among which MCU and EMRE form a subcomplex and function as the conductive channel while MICU1 and MICU2 are EF-hand proteins that regulate the channel activity in a Ca-dependent manner. Here, we present the EM structures of the human mitochondrial calcium uniporter holocomplex (uniplex) in the presence and absence of Ca, revealing distinct Ca dependent assembly of the uniplex. Our structural observations suggest that Ca changes the dimerization interaction between MICU1 and MICU2, which in turn determines how the MICU1-MICU2 subcomplex interacts with the MCU-EMRE channel and, consequently, changes the distribution of the uniplex assemblies between the blocked and unblocked states. | ||||||
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Structure visualization
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| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 6xjv.cif.gz | 702.8 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb6xjv.ent.gz | 571.6 KB | Display | PDB format |
| PDBx/mmJSON format | 6xjv.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 6xjv_validation.pdf.gz | 1.1 MB | Display | wwPDB validaton report |
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| Full document | 6xjv_full_validation.pdf.gz | 1.1 MB | Display | |
| Data in XML | 6xjv_validation.xml.gz | 90.9 KB | Display | |
| Data in CIF | 6xjv_validation.cif.gz | 140.7 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/xj/6xjv ftp://data.pdbj.org/pub/pdb/validation_reports/xj/6xjv | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 22215MC ![]() 6xjxC M: map data used to model this data C: citing same article ( |
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| Similar structure data |
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Assembly
| Deposited unit | ![]()
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Components
| #1: Protein | Mass: 39920.828 Da / Num. of mol.: 8 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#2: Protein | Mass: 11454.140 Da / Num. of mol.: 8 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#3: Protein | Mass: 54432.258 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: MICU1, CALC, CBARA1 / Production host: ![]() #4: Protein | Mass: 49742.141 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: MICU2, EFHA1 / Production host: ![]() |
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-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/MICU1/MICU2 complex / Type: COMPLEX / Details: high calcium state / Entity ID: all / Source: RECOMBINANT |
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| Molecular weight | Value: 0.529 MDa / Experimental value: NO |
| Source (natural) | Organism: Homo sapiens (human) |
| Source (recombinant) | Organism: Homo sapiens (human) |
| Buffer solution | pH: 8 |
| Specimen | Conc.: 1.3 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES / Details: This sample was reconstituted in Msp1 nanodiscs |
| Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 90 % / Chamber temperature: 277 K / Details: blot for 4 seconds before plunging |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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| Microscopy | Model: FEI TITAN KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: SPOT SCAN |
| Electron lens | Mode: BRIGHT FIELD / C2 aperture diameter: 70 µm |
| Specimen holder | Cryogen: NITROGEN |
| Image recording | Average exposure time: 2 sec. / Electron dose: 30.9 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
| EM imaging optics | Energyfilter slit width: 20 eV |
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Processing
| EM software | Name: SerialEM / Category: image acquisition |
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| CTF correction | Type: PHASE FLIPPING ONLY |
| 3D reconstruction | Resolution: 4.17 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 19924 / Symmetry type: POINT |
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About Yorodumi




Homo sapiens (human)
United States, 1items
Citation
UCSF Chimera











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