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Open data
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Basic information
Entry | Database: EMDB / ID: EMD-22042 | |||||||||
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Title | MCU-EMRE complex of a metazoan mitochondrial calcium uniporter | |||||||||
![]() | sharpened map | |||||||||
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![]() | ion channel / calcium channel / mitochondrial calcium uniporter / MCU / EMRE / mitochondria / MEMBRANE PROTEIN | |||||||||
Function / homology | ![]() uniporter activity / uniplex complex / calcium import into the mitochondrion / mitochondrial calcium ion homeostasis / calcium channel activity Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.5 Å | |||||||||
![]() | Long SB / Wang C | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Structure and Reconstitution of an MCU-EMRE Mitochondrial Ca Uniporter Complex. Authors: Chongyuan Wang / Rozbeh Baradaran / Stephen Barstow Long / ![]() Abstract: The proteins MCU and EMRE form the minimal functional unit of the mitochondrial calcium uniporter complex in metazoans, a highly selective and tightly controlled Ca channel of the inner mitochondrial ...The proteins MCU and EMRE form the minimal functional unit of the mitochondrial calcium uniporter complex in metazoans, a highly selective and tightly controlled Ca channel of the inner mitochondrial membrane that regulates cellular metabolism. Here we present functional reconstitution of an MCU-EMRE complex from the red flour beetle, Tribolium castaneum, and a cryo-EM structure of the complex at 3.5 Å resolution. Using a novel assay, we demonstrate robust Ca uptake into proteoliposomes containing the purified complex. Uptake is dependent on EMRE and also on the mitochondrial lipid cardiolipin. The structure reveals a tetrameric channel with a single ion pore. EMRE is located at the periphery of the transmembrane domain and associates primarily with the first transmembrane helix of MCU. Coiled-coil and juxtamembrane domains within the matrix portion of the complex adopt markedly different conformations than in a structure of a human MCU-EMRE complex, suggesting that the structures represent different conformations of these functionally similar metazoan channels. | |||||||||
History |
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Structure visualization
Movie |
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Structure viewer | EM map: ![]() ![]() ![]() |
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 1.5 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 16.9 KB 16.9 KB | Display Display | ![]() |
Images | ![]() | 113 KB | ||
Filedesc metadata | ![]() | 6.1 KB | ||
Others | ![]() | 95.4 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 325.1 KB | Display | ![]() |
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Full document | ![]() | 324.6 KB | Display | |
Data in XML | ![]() | 6.4 KB | Display | |
Data in CIF | ![]() | 7.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6x4sMC M: atomic model generated by this map C: citing same article ( |
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Similar structure data |
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Links
EMDB pages | ![]() ![]() |
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Map
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Annotation | sharpened map | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.088 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Additional map: unsharpened map
File | emd_22042_additional.map | ||||||||||||
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Annotation | unsharpened map | ||||||||||||
Projections & Slices |
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Density Histograms |
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Sample components
-Entire : Mitochondrial Calcium Uniporter (MCU) in complex with EMRE. Embed...
Entire | Name: Mitochondrial Calcium Uniporter (MCU) in complex with EMRE. Embedded in lipid nanodiscs containing cardiolipin. |
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Components |
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-Supramolecule #1: Mitochondrial Calcium Uniporter (MCU) in complex with EMRE. Embed...
Supramolecule | Name: Mitochondrial Calcium Uniporter (MCU) in complex with EMRE. Embedded in lipid nanodiscs containing cardiolipin. type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1 |
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Source (natural) | Organism: ![]() ![]() |
-Macromolecule #1: Calcium uniporter protein,Protein EMRE homolog, mitochondrial-lik...
Macromolecule | Name: Calcium uniporter protein,Protein EMRE homolog, mitochondrial-like Protein fusion type: protein_or_peptide / ID: 1 / Number of copies: 8 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 27.530723 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: GPTAAALERL TTEEVQGLSD VKTLVNQLYE ALNVREHQLQ KEVELTTQLE TLQQELLPLE EKKLELEQVA NRRSNWMAWA GLGLMSVQF GILARLTWWE YSWDIMEPVT YFVTYGTAMA AYAYFVLTRE EYILNDVRDR QQLLLLHKKA KKTGFDVNQY N VLKDQIAK ...String: GPTAAALERL TTEEVQGLSD VKTLVNQLYE ALNVREHQLQ KEVELTTQLE TLQQELLPLE EKKLELEQVA NRRSNWMAWA GLGLMSVQF GILARLTWWE YSWDIMEPVT YFVTYGTAMA AYAYFVLTRE EYILNDVRDR QQLLLLHKKA KKTGFDVNQY N VLKDQIAK LELDLKRLRD PLKLRLPPKA AASGSGSGEN LYFQGSGGLL PEPHRTSFGI IRLILTVVPG LLIGAAISKN IA NFL UniProtKB: Calcium uniporter protein, Essential MCU regulator, mitochondrial |
-Macromolecule #2: CALCIUM ION
Macromolecule | Name: CALCIUM ION / type: ligand / ID: 2 / Number of copies: 1 / Formula: CA |
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Molecular weight | Theoretical: 40.078 Da |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Concentration | 5 mg/mL | ||||||||||||
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Buffer | pH: 7.5 Component:
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Grid | Model: Quantifoil R1.2/1.3 / Material: GOLD / Mesh: 400 / Support film - Material: CARBON / Support film - topology: HOLEY ARRAY / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 10 sec. / Pretreatment - Atmosphere: OTHER | ||||||||||||
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 298 K / Instrument: FEI VITROBOT MARK IV / Details: 2 second blot, blot force of 0. | ||||||||||||
Details | Monodisperse sample |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: SUPER-RESOLUTION / Digitization - Frames/image: 1-40 / Number grids imaged: 3 / Number real images: 8143 / Average exposure time: 0.25 sec. / Average electron dose: 1.9 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: -3.0 µm / Nominal defocus min: -1.0 µm / Nominal magnification: 22500 |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
-Atomic model buiding 1
Refinement | Space: REAL / Protocol: AB INITIO MODEL / Overall B value: 127 / Target criteria: Correlation coefficient |
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Output model | ![]() PDB-6x4s: |