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- EMDB-40566: human liver mitochondrial Superoxide dismutase [Mn] -

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Basic information

Entry
Database: EMDB / ID: EMD-40566
Titlehuman liver mitochondrial Superoxide dismutase [Mn]
Map data
Sample
  • Complex: Superoxide dismutase [Mn]
    • Protein or peptide: Superoxide dismutase [Mn], mitochondrial
  • Ligand: MANGANESE (II) ION
Keywordshuman / liver / mitochondrial / Superoxide dismutase [Mn] / OXIDOREDUCTASE
Function / homology
Function and homology information


acetylcholine-mediated vasodilation involved in regulation of systemic arterial blood pressure / negative regulation of membrane hyperpolarization / : / positive regulation of hydrogen peroxide biosynthetic process / response to magnetism / response to silicon dioxide / response to selenium ion / response to L-ascorbic acid / intracellular oxygen homeostasis / response to superoxide ...acetylcholine-mediated vasodilation involved in regulation of systemic arterial blood pressure / negative regulation of membrane hyperpolarization / : / positive regulation of hydrogen peroxide biosynthetic process / response to magnetism / response to silicon dioxide / response to selenium ion / response to L-ascorbic acid / intracellular oxygen homeostasis / response to superoxide / response to manganese ion / hydrogen peroxide biosynthetic process / response to zinc ion / superoxide metabolic process / positive regulation of vascular associated smooth muscle cell apoptotic process / superoxide dismutase / Detoxification of Reactive Oxygen Species / Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer's disease models / superoxide dismutase activity / response to isolation stress / response to immobilization stress / negative regulation of vascular associated smooth muscle cell proliferation / mitochondrial nucleoid / response to electrical stimulus / cellular response to ethanol / response to cadmium ion / FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes / Mitochondrial unfolded protein response (UPRmt) / negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway / removal of superoxide radicals / release of cytochrome c from mitochondria / Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation / response to activity / response to hydrogen peroxide / Transcriptional activation of mitochondrial biogenesis / oxygen binding / regulation of blood pressure / manganese ion binding / response to lipopolysaccharide / cellular response to oxidative stress / negative regulation of neuron apoptotic process / protein homotetramerization / response to hypoxia / response to xenobiotic stimulus / positive regulation of cell migration / mitochondrial matrix / negative regulation of cell population proliferation / regulation of transcription by RNA polymerase II / enzyme binding / mitochondrion / DNA binding / extracellular exosome / identical protein binding
Similarity search - Function
: / Manganese/iron superoxide dismutase, binding site / Manganese and iron superoxide dismutases signature. / Manganese/iron superoxide dismutase / Manganese/iron superoxide dismutase, N-terminal / Iron/manganese superoxide dismutases, alpha-hairpin domain / Manganese/iron superoxide dismutase, C-terminal / Manganese/iron superoxide dismutase, C-terminal domain superfamily / Manganese/iron superoxide dismutase, N-terminal domain superfamily / Iron/manganese superoxide dismutases, C-terminal domain
Similarity search - Domain/homology
Superoxide dismutase [Mn], mitochondrial
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.91 Å
AuthorsZhang Z / Tringides M
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)R01AI145069 United States
CitationJournal: Mol Cell Proteomics / Year: 2023
Title: High-Resolution Structural Proteomics of Mitochondria Using the 'Build and Retrieve' Methodology.
Authors: Zhemin Zhang / Marios L Tringides / Christopher E Morgan / Masaru Miyagi / Jason A Mears / Charles L Hoppel / Edward W Yu /
Abstract: The application of integrated systems biology to the field of structural biology is a promising new direction, although it is still in the infant stages of development. Here we report the use of ...The application of integrated systems biology to the field of structural biology is a promising new direction, although it is still in the infant stages of development. Here we report the use of single particle cryo-EM to identify multiple proteins from three enriched heterogeneous fractions prepared from human liver mitochondrial lysate. We simultaneously identify and solve high-resolution structures of nine essential mitochondrial enzymes with key metabolic functions, including fatty acid catabolism, reactive oxidative species clearance, and amino acid metabolism. Our methodology also identified multiple distinct members of the acyl-CoA dehydrogenase family. This work highlights the potential of cryo-EM to explore tissue proteomics at the atomic level.
History
DepositionApr 20, 2023-
Header (metadata) releaseFeb 21, 2024-
Map releaseFeb 21, 2024-
UpdateMay 21, 2025-
Current statusMay 21, 2025Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_40566.png

Downloads & links

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Map

FileDownload / File: emd_40566.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
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AxesZ (Sec.)Y (Row.)X (Col.)
1.07 Å/pix.
x 256 pix.
= 273.92 Å		1.07 Å/pix.
x 256 pix.
= 273.92 Å		1.07 Å/pix.
x 256 pix.
= 273.92 Å

Surface

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Images are generated by Spider.

Voxel sizeX=Y=Z: 1.07 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.1
Minimum - Maximum-0.380206 - 0.8492592
Average (Standard dev.)-0.00028982636 (±0.018538805)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions256256256
Spacing256256256
CellA=B=C: 273.92 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #1

Fileemd_40566_half_map_1.map
Projections & Slices
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Histogram

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Half map: #2

Fileemd_40566_half_map_2.map
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Sample components

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Entire : Superoxide dismutase [Mn]

EntireName: Superoxide dismutase [Mn]
Components
  • Complex: Superoxide dismutase [Mn]
    • Protein or peptide: Superoxide dismutase [Mn], mitochondrial
  • Ligand: MANGANESE (II) ION

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Supramolecule #1: Superoxide dismutase [Mn]

SupramoleculeName: Superoxide dismutase [Mn] / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: Superoxide dismutase [Mn], mitochondrial

MacromoleculeName: Superoxide dismutase [Mn], mitochondrial / type: protein_or_peptide / ID: 1 / Number of copies: 4 / Enantiomer: LEVO / EC number: superoxide dismutase
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 24.782119 KDa
SequenceString: MLSRAVCGTS RQLAPVLGYL GSRQKHSLPD LPYDYGALEP HINAQIMQLH HSKHHAAYVN NLNVTEEKYQ EALAKGDVTA QIALQPALK FNGGGHINHS IFWTNLSPNG GGEPKGELLE AIKRDFGSFD KFKEKLTAAS VGVQGSGWGW LGFNKERGHL Q IAACPNQD ...String:
MLSRAVCGTS RQLAPVLGYL GSRQKHSLPD LPYDYGALEP HINAQIMQLH HSKHHAAYVN NLNVTEEKYQ EALAKGDVTA QIALQPALK FNGGGHINHS IFWTNLSPNG GGEPKGELLE AIKRDFGSFD KFKEKLTAAS VGVQGSGWGW LGFNKERGHL Q IAACPNQD PLQGTTGLIP LLGIDVWEHA YYLQYKNVRP DYLKAIWNVI NWENVTERYM ACKK

UniProtKB: Superoxide dismutase [Mn], mitochondrial

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Macromolecule #2: MANGANESE (II) ION

MacromoleculeName: MANGANESE (II) ION / type: ligand / ID: 2 / Number of copies: 4 / Formula: MN
Molecular weightTheoretical: 54.938 Da

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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: 7.5
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 39.5 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.5 µm / Nominal defocus min: 0.8 µm / Nominal magnification: 81000
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: INSILICO MODEL
Final reconstructionResolution.type: BY AUTHOR / Resolution: 2.91 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 50014
Initial angle assignmentType: ANGULAR RECONSTITUTION
Final angle assignmentType: ANGULAR RECONSTITUTION
FSC plot (resolution estimation)

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