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- EMDB-15866: Cryo-EM structure of succinate dehydrogenase complex (complex-II)... -
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Open data
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Basic information
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Title | Cryo-EM structure of succinate dehydrogenase complex (complex-II) in respiratory supercomplex of Tetrahymena thermophila | |||||||||||||||
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Function / homology | ![]() : / mitochondrial electron transport, succinate to ubiquinone / succinate dehydrogenase / succinate dehydrogenase (quinone) activity / anaerobic respiration / 3 iron, 4 sulfur cluster binding / tricarboxylic acid cycle / respiratory electron transport chain / 2 iron, 2 sulfur cluster binding / flavin adenine dinucleotide binding ...: / mitochondrial electron transport, succinate to ubiquinone / succinate dehydrogenase / succinate dehydrogenase (quinone) activity / anaerobic respiration / 3 iron, 4 sulfur cluster binding / tricarboxylic acid cycle / respiratory electron transport chain / 2 iron, 2 sulfur cluster binding / flavin adenine dinucleotide binding / 4 iron, 4 sulfur cluster binding / electron transfer activity / mitochondrial inner membrane / membrane / plasma membrane Similarity search - Function | |||||||||||||||
Biological species | ![]() ![]() | |||||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.0 Å | |||||||||||||||
![]() | Muhleip A / Kock Flygaard R / Baradaran R / Amunts A | |||||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Structural basis of mitochondrial membrane bending by the I-II-III-IV supercomplex. Authors: Alexander Mühleip / Rasmus Kock Flygaard / Rozbeh Baradaran / Outi Haapanen / Thomas Gruhl / Victor Tobiasson / Amandine Maréchal / Vivek Sharma / Alexey Amunts / ![]() ![]() ![]() ![]() ![]() Abstract: Mitochondrial energy conversion requires an intricate architecture of the inner mitochondrial membrane. Here we show that a supercomplex containing all four respiratory chain components contributes ...Mitochondrial energy conversion requires an intricate architecture of the inner mitochondrial membrane. Here we show that a supercomplex containing all four respiratory chain components contributes to membrane curvature induction in ciliates. We report cryo-electron microscopy and cryo-tomography structures of the supercomplex that comprises 150 different proteins and 311 bound lipids, forming a stable 5.8-MDa assembly. Owing to subunit acquisition and extension, complex I associates with a complex IV dimer, generating a wedge-shaped gap that serves as a binding site for complex II. Together with a tilted complex III dimer association, it results in a curved membrane region. Using molecular dynamics simulations, we demonstrate that the divergent supercomplex actively contributes to the membrane curvature induction and tubulation of cristae. Our findings highlight how the evolution of protein subunits of respiratory complexes has led to the I-II-III-IV supercomplex that contributes to the shaping of the bioenergetic membrane, thereby enabling its functional specialization. #1: ![]() Title: Structural basis of mitochondrial membrane bending by I-II-III2-IV2 supercomplex Authors: Muhleip A / Flygaard RK / Haapanen O / Baradaran R / Gruhl T / Tobiasson V / Marechal A / Sharma V / Amunts A | |||||||||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 398.5 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 35 KB 35 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 16.5 KB | Display | ![]() |
Images | ![]() | 62.8 KB | ||
Masks | ![]() | 421.9 MB | ![]() | |
Others | ![]() ![]() ![]() | 213 MB 390.9 MB 390.9 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8b6gMC ![]() 8b6fC ![]() 8b6hC ![]() 8b6jC M: atomic model generated by this map C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Annotation | Sharpened mask refined map | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.25 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Mask #1
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-Additional map: Unsharpened mask refined map
File | emd_15866_additional_1.map | ||||||||||||
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Annotation | Unsharpened mask refined map | ||||||||||||
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Density Histograms |
-Half map: Half-map A
File | emd_15866_half_map_1.map | ||||||||||||
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Annotation | Half-map A | ||||||||||||
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-Half map: Half-map B
File | emd_15866_half_map_2.map | ||||||||||||
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Annotation | Half-map B | ||||||||||||
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Sample components
+Entire : Succinate dehydrogenase complex (complex-II)
+Supramolecule #1: Succinate dehydrogenase complex (complex-II)
+Macromolecule #1: Diphthamide synthesis protein
+Macromolecule #2: Transmembrane protein, putative
+Macromolecule #3: Transposase
+Macromolecule #4: Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitoch...
+Macromolecule #5: DUF4885 domain-containing protein
+Macromolecule #6: Succinate dehydrogenase (quinone)
+Macromolecule #7: Transmembrane protein, putative
+Macromolecule #8: SDHTT3
+Macromolecule #9: Transmembrane protein, putative
+Macromolecule #10: NmrA domain-containing protein
+Macromolecule #11: Transmembrane protein, putative
+Macromolecule #12: Transmembrane protein, putative
+Macromolecule #13: Cytochrome b-c1 complex subunit 8
+Macromolecule #14: SDHTT11
+Macromolecule #15: SDHD
+Macromolecule #16: CARDIOLIPIN
+Macromolecule #17: CALCIUM ION
+Macromolecule #18: FLAVIN-ADENINE DINUCLEOTIDE
+Macromolecule #19: FE2/S2 (INORGANIC) CLUSTER
+Macromolecule #20: IRON/SULFUR CLUSTER
+Macromolecule #21: FE3-S4 CLUSTER
+Macromolecule #22: 1,2-Distearoyl-sn-glycerophosphoethanolamine
+Macromolecule #23: HEME C
+Macromolecule #24: 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE
+Macromolecule #25: Ubiquinone-8
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.5 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K2 QUANTUM (4k x 4k) / Average electron dose: 25.66 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.6 µm / Nominal defocus min: 0.6 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |