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Yorodumi- EMDB-22290: Structure of a mitochondrial calcium uniporter holocomplex (MICU1... -
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Open data
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Basic information
| Entry | Database: EMDB / ID: EMD-22290 | |||||||||
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| Title | Structure of a mitochondrial calcium uniporter holocomplex (MICU1, MICU2, MCU, EMRE) in low Ca2+ | |||||||||
Map data | main map. Sharpened | |||||||||
Sample |
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Keywords | ion channel / calcium channel / mitochondrial calcium uniporter / MCU / EMRE / mitochondria / TRANSPORT PROTEIN-CALCIUM BINDING PROTEIN complex | |||||||||
| 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 / cellular response to calcium ion starvation / calcium ion import / calcium channel inhibitor activity / calcium channel complex / Mitochondrial protein degradation / cellular response to calcium ion / calcium channel regulator activity / defense response / protein homooligomerization / mitochondrial membrane / calcium channel activity / mitochondrial intermembrane space / mitochondrial inner membrane / protein heterodimerization activity / calcium ion binding / mitochondrion / metal ion binding / identical protein binding Similarity search - Function | |||||||||
| Biological species | ![]() Homo sapiens (human) | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.3 Å | |||||||||
Authors | Long SB / Wang C | |||||||||
| Funding support | United States, 2 items
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Citation | Journal: Elife / Year: 2020Title: Structures reveal gatekeeping of the mitochondrial Ca uniporter by MICU1-MICU2. Authors: Chongyuan Wang / Agata Jacewicz / Bryce D Delgado / Rozbeh Baradaran / Stephen Barstow Long / ![]() Abstract: The mitochondrial calcium uniporter is a Ca-gated ion channel complex that controls mitochondrial Ca entry and regulates cell metabolism. MCU and EMRE form the channel while Ca-dependent regulation ...The mitochondrial calcium uniporter is a Ca-gated ion channel complex that controls mitochondrial Ca entry and regulates cell metabolism. MCU and EMRE form the channel while Ca-dependent regulation is conferred by MICU1 and MICU2 through an enigmatic process. We present a cryo-EM structure of an MCU-EMRE-MICU1-MICU2 holocomplex comprising MCU and EMRE subunits from the beetle Tribolium castaneum in complex with a human MICU1-MICU2 heterodimer at 3.3 Å resolution. With analogy to how neuronal channels are blocked by protein toxins, a uniporter interaction domain on MICU1 binds to a channel receptor site comprising MCU and EMRE subunits to inhibit ion flow under resting Ca conditions. A Ca-bound structure of MICU1-MICU2 at 3.1 Å resolution indicates how Ca-dependent changes enable dynamic response to cytosolic Ca signals. | |||||||||
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Structure visualization
| Movie |
Movie viewer |
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| Structure viewer | EM map: SurfView Molmil Jmol/JSmol |
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_22290.map.gz | 74.9 MB | EMDB map data format | |
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| Header (meta data) | emd-22290-v30.xml emd-22290.xml | 24 KB 24 KB | Display Display | EMDB header |
| Images | emd_22290.png | 65.7 KB | ||
| Filedesc metadata | emd-22290.cif.gz | 6.9 KB | ||
| Others | emd_22290_additional_1.map.gz emd_22290_additional_2.map.gz | 3 MB 2.8 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-22290 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-22290 | HTTPS FTP |
-Validation report
| Summary document | emd_22290_validation.pdf.gz | 480 KB | Display | EMDB validaton report |
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| Full document | emd_22290_full_validation.pdf.gz | 479.6 KB | Display | |
| Data in XML | emd_22290_validation.xml.gz | 6.2 KB | Display | |
| Data in CIF | emd_22290_validation.cif.gz | 7.1 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-22290 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-22290 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 6xqnMC ![]() 6xqoC C: citing same article ( M: atomic model generated by this map |
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| Similar structure data |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_22290.map.gz / Format: CCP4 / Size: 103 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Annotation | main map. Sharpened | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.064 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Additional map: sharpened map calculated from the first 6 frames.
| File | emd_22290_additional_1.map | ||||||||||||
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| Annotation | sharpened map calculated from the first 6 frames. | ||||||||||||
| Projections & Slices |
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| Density Histograms |
-Additional map: unsharpened map
| File | emd_22290_additional_2.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 holocomplex
| Entire | Name: Mitochondrial Calcium Uniporter holocomplex |
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| Components |
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-Supramolecule #1: Mitochondrial Calcium Uniporter holocomplex
| Supramolecule | Name: Mitochondrial Calcium Uniporter holocomplex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#4 |
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-Supramolecule #2: EMRE
| Supramolecule | Name: EMRE / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1 |
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| Source (natural) | Organism: ![]() |
-Supramolecule #3: MCU
| Supramolecule | Name: MCU / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #2 |
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| Source (natural) | Organism: ![]() |
-Supramolecule #4: MICU1-MICU2 heterodimer
| Supramolecule | Name: MICU1-MICU2 heterodimer / type: complex / ID: 4 / Parent: 1 / Macromolecule list: #3-#4 |
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| Source (natural) | Organism: Homo sapiens (human) |
-Macromolecule #1: Protein EMRE homolog, mitochondrial-like Protein
| Macromolecule | Name: Protein EMRE homolog, mitochondrial-like Protein / type: protein_or_peptide / ID: 1 / Number of copies: 3 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 7.37219 KDa |
| Recombinant expression | Organism: Homo sapiens (human) |
| Sequence | String: GPTAAALETA VYSKSGGLLP EPHRTSFGII RLILTVVPGL LIGAAISKNI ANFLEENDLF VPSDDDDDDD UniProtKB: Essential MCU regulator, mitochondrial |
-Macromolecule #2: Calcium uniporter protein
| Macromolecule | Name: Calcium uniporter protein / type: protein_or_peptide / ID: 2 / Number of copies: 4 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 23.6341 KDa |
| Recombinant expression | Organism: Homo sapiens (human) |
| 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 AAKEEGGWSH PQFEK UniProtKB: Calcium uniporter protein, mitochondrial |
-Macromolecule #3: Calcium uptake protein 1, mitochondrial
| Macromolecule | Name: Calcium uptake protein 1, mitochondrial / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO |
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| Source (natural) | Organism: Homo sapiens (human) |
| Molecular weight | Theoretical: 45.422883 KDa |
| Recombinant expression | Organism: Homo sapiens (human) |
| Sequence | String: GPTAAALEPH PEEKKKKRSG FRDRKVMEYE NRIRAYSTPD KIFRYFATLK VISEPGEAEV FMTPEDFVRS ITPNEKQPEH LGLDQYIIK RFDGKKISQE REKFADEGSI FYTLGECGLI SFSDYIFLTT VLSTPQRNFE IAFKMFDLNG DGEVDMEEFE Q VQSIIRSQ ...String: GPTAAALEPH PEEKKKKRSG FRDRKVMEYE NRIRAYSTPD KIFRYFATLK VISEPGEAEV FMTPEDFVRS ITPNEKQPEH LGLDQYIIK RFDGKKISQE REKFADEGSI FYTLGECGLI SFSDYIFLTT VLSTPQRNFE IAFKMFDLNG DGEVDMEEFE Q VQSIIRSQ TSMGMRHRDR PTTGNTLKSG LCSALTTYFF GADLKGKLTI KNFLEFQRKL QHDVLKLEFE RHDPVDGRIT ER QFGGMLL AYSGVQSKKL TAMQRQLKKH FKEGKGLTFQ EVENFFTFLK NINDVDTALS FYHMAGASLD KVTMQQVART VAK VELSDH VCDVVFALFD CDGNGELSNK EFVSIMKQRL MRGLEKPKDM GFTRLMQAMW KCAQETAWDF ALPKQSNW UniProtKB: Calcium uptake protein 1, mitochondrial |
-Macromolecule #4: Calcium uptake protein 2, mitochondrial
| Macromolecule | Name: Calcium uptake protein 2, mitochondrial / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO |
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| Source (natural) | Organism: Homo sapiens (human) |
| Molecular weight | Theoretical: 44.980609 KDa |
| Recombinant expression | Organism: Homo sapiens (human) |
| Sequence | String: HHSRVSVAAR DGSFTVSAQK NVEHGIIYIG KPSLRKQRFM QFSSLEHEGE YYMTPRDFLF SVMFEQMERK TSVKKLTKKD IEDTLSGIQ TAGCGSTFFR DLGDKGLISY TEYLFLLTIL TKPHSGFHVA FKMLDTDGNE MIEKREFFKL QKIISKQDDL M TVKTNETG ...String: HHSRVSVAAR DGSFTVSAQK NVEHGIIYIG KPSLRKQRFM QFSSLEHEGE YYMTPRDFLF SVMFEQMERK TSVKKLTKKD IEDTLSGIQ TAGCGSTFFR DLGDKGLISY TEYLFLLTIL TKPHSGFHVA FKMLDTDGNE MIEKREFFKL QKIISKQDDL M TVKTNETG YQEAIVKEPE INTTLQMRFF GKRGQRKLHY KEFRRFMENL QTEIQEMEFL QFSKGLSFMR KEDFAEWLLF FT NTENKDI YWKNVREKLS AGESISLDEF KSFCHFTTHL EDFAIAMQMF SLAHRPVRLA EFKRAVKVAT GQELSNNILD TVF KIFDLD GDECLSHEEF LGVLKNRMHR GLWVPQHQSI QEYWKCVKKE SIKGVKEVWK QAGKGLF UniProtKB: Calcium uptake protein 2, mitochondrial |
-Macromolecule #5: CALCIUM ION
| Macromolecule | Name: CALCIUM ION / type: ligand / ID: 5 / 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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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Concentration | 1.0 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 | ||||||||||||
| 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 K3 BIOQUANTUM (6k x 4k) / Detector mode: SUPER-RESOLUTION / Digitization - Frames/image: 1-40 / Number grids imaged: 5 / Number real images: 21115 / Average exposure time: 4.0 sec. / Average electron dose: 71.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| 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: 124 / Target criteria: Correlation coefficient |
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| Output model | ![]() PDB-6xqn: |
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About Yorodumi


Keywords
Homo sapiens (human)
Authors
United States, 2 items
Citation
UCSF Chimera












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