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- EMDB-77084: MCU-EMRE complex with spermine -

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Basic information

Entry
Database: EMDB / ID: EMD-77084
TitleMCU-EMRE complex with spermine
Map dataHuman MCU-EMRE complex in the presence of spermine
Sample
  • Complex: MCU-EMRE complex with spermine
    • Protein or peptide: Essential MCU regulator, mitochondrial
    • Protein or peptide: Calcium uniporter protein, mitochondrial
  • Ligand: CALCIUM ION
  • Ligand: O-[(R)-{[(2R)-2,3-bis(octadecanoyloxy)propyl]oxy}(hydroxy)phosphoryl]-L-serine
  • Ligand: CARDIOLIPIN
  • Ligand: SPERMINE
Keywordsmitochondrial calcium uniporter / MCU / EMRE / MEMBRANE PROTEIN
Function / homology
Function and homology information


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 ...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
Essential MCU regulator, mitochondrial / Putative mitochondrial precursor protein / Calcium uniporter protein, C-terminal / MCU family / Mitochondrial calcium uniporter
Similarity search - Domain/homology
Calcium uniporter protein, mitochondrial / Essential MCU regulator, mitochondrial
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.98 Å
AuthorsWang Q / Balderas E / Rai NK / Cao E / Chaudhuri D
Funding support United States, 3 items
OrganizationGrant numberCountry
National Institutes of Health/National Heart, Lung, and Blood Institute (NIH/NHLBI)R01HL165797 United States
National Institutes of Health/National Heart, Lung, and Blood Institute (NIH/NHLBI)R01HL141353 United States
National Institutes of Health/National Heart, Lung, and Blood Institute (NIH/NHLBI)R01DK143101 United States
CitationJournal: To Be Published
Title: MCU-EMRE complex with spermine
Authors: Wang Q / Balderas E / Rai NK / Cao E / Chaudhuri D
History
DepositionMay 7, 2026-
Header (metadata) releaseJul 8, 2026-
Map releaseJul 8, 2026-
UpdateJul 8, 2026-
Current statusJul 8, 2026Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

Downloads & links

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Map

FileReleased
AnnotationHuman MCU-EMRE complex in the presence of spermine
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.73 Å/pix.
x 384 pix.
= 280.166 Å
0.73 Å/pix.
x 384 pix.
= 280.166 Å
0.73 Å/pix.
x 384 pix.
= 280.166 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.7296 Å
Density
Contour LevelBy AUTHOR: 0.11
Minimum - Maximum-0.84164524 - 1.4541596
Average (Standard dev.)0.00038406983 (±0.027764315)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions384384384
Spacing384384384
CellA=B=C: 280.1664 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: Human MCU-EMRE complex in the presence of spermine, half map1

Fileemd_77084_half_map_1.map
AnnotationHuman MCU-EMRE complex in the presence of spermine, half map1
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Half map: Human MCU-EMRE complex in the presence of spermine, half map2

Fileemd_77084_half_map_2.map
AnnotationHuman MCU-EMRE complex in the presence of spermine, half map2
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Sample components

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Entire : MCU-EMRE complex with spermine

EntireName: MCU-EMRE complex with spermine
Components
  • Complex: MCU-EMRE complex with spermine
    • Protein or peptide: Essential MCU regulator, mitochondrial
    • Protein or peptide: Calcium uniporter protein, mitochondrial
  • Ligand: CALCIUM ION
  • Ligand: O-[(R)-{[(2R)-2,3-bis(octadecanoyloxy)propyl]oxy}(hydroxy)phosphoryl]-L-serine
  • Ligand: CARDIOLIPIN
  • Ligand: SPERMINE

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Supramolecule #1: MCU-EMRE complex with spermine

SupramoleculeName: MCU-EMRE complex with spermine / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: Essential MCU regulator, mitochondrial

MacromoleculeName: Essential MCU regulator, mitochondrial / type: protein_or_peptide / ID: 1 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 5.864078 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString:
VIVTRSGAIL PKPVKMSFGL LRVFSIVIPF LYVGTLISKN FAALLEEHDI FVP

UniProtKB: Essential MCU regulator, mitochondrial

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Macromolecule #2: Calcium uniporter protein, mitochondrial

MacromoleculeName: Calcium uniporter protein, mitochondrial / type: protein_or_peptide / ID: 2 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 20.502756 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString:
AATLNDVKTL VQQLYTTLCI EQHQLNKERE LIERLEDLKE QLAPLEKVRI EISRKAEKRT TLVLWGGLAY MATQFGILAR LTWWEYSWD IMEPVTYFIT YGSAMAMYAY FVMTRQEYVY PEARDRQYLL FFHKGAKKSR FDLEKYNQLK DAIAQAEMDL K RLRDPLQV HLPL

UniProtKB: Calcium uniporter protein, mitochondrial

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Macromolecule #3: CALCIUM ION

MacromoleculeName: CALCIUM ION / type: ligand / ID: 3 / Number of copies: 2 / Formula: CA
Molecular weightTheoretical: 40.078 Da

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Macromolecule #4: O-[(R)-{[(2R)-2,3-bis(octadecanoyloxy)propyl]oxy}(hydroxy)phospho...

MacromoleculeName: O-[(R)-{[(2R)-2,3-bis(octadecanoyloxy)propyl]oxy}(hydroxy)phosphoryl]-L-serine
type: ligand / ID: 4 / Number of copies: 4 / Formula: P5S
Molecular weightTheoretical: 792.075 Da
Chemical component information

ChemComp-P5S:
O-[(R)-{[(2R)-2,3-bis(octadecanoyloxy)propyl]oxy}(hydroxy)phosphoryl]-L-serine

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Macromolecule #5: CARDIOLIPIN

MacromoleculeName: CARDIOLIPIN / type: ligand / ID: 5 / Number of copies: 4 / Formula: CDL
Molecular weightTheoretical: 1.464043 KDa
Chemical component information

ChemComp-CDL:
CARDIOLIPIN / phospholipid*YM

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Macromolecule #6: SPERMINE

MacromoleculeName: SPERMINE / type: ligand / ID: 6 / Number of copies: 1 / Formula: SPM
Molecular weightTheoretical: 202.34 Da
Chemical component information

ChemComp-SPM:
SPERMINE

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.4
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: TFS FALCON 4i (4k x 4k) / Average electron dose: 45.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 0.5 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: OTHER
Details: Initial model was calculated using cryosparc ab initial methods
Final reconstructionResolution.type: BY AUTHOR / Resolution: 2.98 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 84413
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD

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Atomic model buiding 1

RefinementProtocol: AB INITIO MODEL
Output model

PDB-13io:
MCU-EMRE complex with spermine

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