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- EMDB-35315: Respiratory complex Membrane domain of CI, focused map of type I,... -
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Open data
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Basic information
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Title | Respiratory complex Membrane domain of CI, focused map of type I, Wild type mouse under thermoneutral temperature | |||||||||
![]() | Focus-refined map, Membrane Domain, Thermoneutral, Type I of Respiratory Supercomplex CI:CIII2 | |||||||||
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![]() | Respiratory complex / Respiratory supercomplex / ELECTRON TRANSPORT | |||||||||
Function / homology | ![]() Mitochondrial protein import / Protein lipoylation / Mitochondrial Fatty Acid Beta-Oxidation / Complex I biogenesis / Respiratory electron transport / cellular response to oxygen levels / mitochondrial [2Fe-2S] assembly complex / iron-sulfur cluster assembly complex / mitochondrial large ribosomal subunit binding / gliogenesis ...Mitochondrial protein import / Protein lipoylation / Mitochondrial Fatty Acid Beta-Oxidation / Complex I biogenesis / Respiratory electron transport / cellular response to oxygen levels / mitochondrial [2Fe-2S] assembly complex / iron-sulfur cluster assembly complex / mitochondrial large ribosomal subunit binding / gliogenesis / negative regulation of non-canonical NF-kappaB signal transduction / neural precursor cell proliferation / [2Fe-2S] cluster assembly / positive regulation of mitochondrial membrane potential / oxygen sensor activity / iron-sulfur cluster assembly / positive regulation of ATP biosynthetic process / NADH:ubiquinone reductase (H+-translocating) / NADH dehydrogenase activity / mitochondrial electron transport, NADH to ubiquinone / mitochondrial respiratory chain complex I assembly / proton motive force-driven mitochondrial ATP synthesis / respiratory chain complex I / NADH dehydrogenase (ubiquinone) activity / quinone binding / ATP synthesis coupled electron transport / negative regulation of reactive oxygen species biosynthetic process / Neutrophil degranulation / cerebellum development / reactive oxygen species metabolic process / aerobic respiration / neurogenesis / response to nicotine / response to cocaine / electron transport chain / response to hydrogen peroxide / mitochondrial intermembrane space / NAD binding / fatty acid biosynthetic process / myelin sheath / 4 iron, 4 sulfur cluster binding / response to ethanol / in utero embryonic development / response to hypoxia / mitochondrial inner membrane / nuclear speck / mitochondrial matrix / ubiquitin protein ligase binding / protein-containing complex binding / mitochondrion / nucleoplasm / metal ion binding Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.4 Å | |||||||||
![]() | Shin Y-C / Liao M | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Structural basis of respiratory complex adaptation to cold temperatures. Authors: Young-Cheul Shin / Pedro Latorre-Muro / Amina Djurabekova / Oleksii Zdorevskyi / Christopher F Bennett / Nils Burger / Kangkang Song / Chen Xu / Joao A Paulo / Steven P Gygi / Vivek Sharma / ...Authors: Young-Cheul Shin / Pedro Latorre-Muro / Amina Djurabekova / Oleksii Zdorevskyi / Christopher F Bennett / Nils Burger / Kangkang Song / Chen Xu / Joao A Paulo / Steven P Gygi / Vivek Sharma / Maofu Liao / Pere Puigserver / ![]() ![]() ![]() Abstract: In response to cold, mammals activate brown fat for respiratory-dependent thermogenesis reliant on the electron transport chain. Yet, the structural basis of respiratory complex adaptation upon cold ...In response to cold, mammals activate brown fat for respiratory-dependent thermogenesis reliant on the electron transport chain. Yet, the structural basis of respiratory complex adaptation upon cold exposure remains elusive. Herein, we combined thermoregulatory physiology and cryoelectron microscopy (cryo-EM) to study endogenous respiratory supercomplexes from mice exposed to different temperatures. A cold-induced conformation of CI:III (termed type 2) supercomplex was identified with a ∼25° rotation of CIII around its inter-dimer axis, shortening inter-complex Q exchange space, and exhibiting catalytic states that favor electron transfer. Large-scale supercomplex simulations in mitochondrial membranes reveal how lipid-protein arrangements stabilize type 2 complexes to enhance catalytic activity. Together, our cryo-EM studies, multiscale simulations, and biochemical analyses unveil the thermoregulatory mechanisms and dynamics of increased respiratory capacity in brown fat at the structural and energetic level. | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 197.2 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 40.8 KB 40.8 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 12.7 KB | Display | ![]() |
Images | ![]() | 104.7 KB | ||
Masks | ![]() | 216 MB | ![]() | |
Filedesc metadata | ![]() | 9.7 KB | ||
Others | ![]() ![]() | 193.7 MB 193.7 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 1.1 MB | Display | ![]() |
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Full document | ![]() | 1.1 MB | Display | |
Data in XML | ![]() | 21.6 KB | Display | |
Data in CIF | ![]() | 28.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8iaqMC ![]() 8iaoC ![]() 8iapC ![]() 8iarC ![]() 8ib4C ![]() 8ib5C ![]() 8ib6C ![]() 8ib7C ![]() 8ib9C ![]() 8ibaC ![]() 8ibbC ![]() 8ibcC ![]() 8ibdC ![]() 8ibeC ![]() 8ibfC ![]() 8ibgC ![]() 8ic2C ![]() 8ic3C ![]() 8ic4C ![]() 8ic5C ![]() 8xnlC ![]() 8xnmC ![]() 8xnnC ![]() 8xnoC ![]() 8xnpC ![]() 8xnqC ![]() 8xnrC ![]() 8xnsC ![]() 8xntC ![]() 8xnuC ![]() 8xnvC ![]() 8xnwC ![]() 8xnxC ![]() 8xnyC ![]() 8xnzC ![]() 8xo0C 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 | Focus-refined map, Membrane Domain, Thermoneutral, Type I of Respiratory Supercomplex CI:CIII2 | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.1 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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Projections & Slices |
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Density Histograms |
-Half map: Focus-refined map, Membrane Domain, Thermoneutral, Type I of...
File | emd_35315_half_map_1.map | ||||||||||||
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Annotation | Focus-refined map, Membrane Domain, Thermoneutral, Type I of Respiratory Supercomplex CI:CIII2 | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Focus-refined map, Membrane Domain, Thermoneutral, Type I of...
File | emd_35315_half_map_2.map | ||||||||||||
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Annotation | Focus-refined map, Membrane Domain, Thermoneutral, Type I of Respiratory Supercomplex CI:CIII2 | ||||||||||||
Projections & Slices |
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Density Histograms |
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Sample components
+Entire : Respiratory complex
+Supramolecule #1: Respiratory complex
+Macromolecule #1: NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial
+Macromolecule #2: NADH-ubiquinone oxidoreductase chain 6
+Macromolecule #3: NADH-ubiquinone oxidoreductase chain 4L
+Macromolecule #4: NADH-ubiquinone oxidoreductase chain 5
+Macromolecule #5: NADH-ubiquinone oxidoreductase chain 4
+Macromolecule #6: NADH-ubiquinone oxidoreductase chain 2
+Macromolecule #7: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mi...
+Macromolecule #8: Acyl carrier protein, mitochondrial
+Macromolecule #9: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8
+Macromolecule #10: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 11
+Macromolecule #11: NADH dehydrogenase [ubiquinone] 1 subunit C1, mitochondrial
+Macromolecule #12: NADH dehydrogenase [ubiquinone] 1 subunit C2
+Macromolecule #13: NADH dehydrogenase [ubiquinone] iron-sulfur protein 5
+Macromolecule #14: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 1
+Macromolecule #15: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 11, mit...
+Macromolecule #16: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 5, mito...
+Macromolecule #17: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 6
+Macromolecule #18: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 2, mito...
+Macromolecule #19: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3
+Macromolecule #20: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mito...
+Macromolecule #21: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4
+Macromolecule #22: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9
+Macromolecule #23: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7
+Macromolecule #24: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10
+Macromolecule #25: 1,2-Distearoyl-sn-glycerophosphoethanolamine
+Macromolecule #26: CARDIOLIPIN
+Macromolecule #27: 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE
+Macromolecule #28: ADENOSINE-5'-DIPHOSPHATE
+Macromolecule #29: ~{S}-[2-[3-[[(2~{R})-3,3-dimethyl-2-oxidanyl-4-phosphonooxy-butan...
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Concentration | 0.33 mg/mL |
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Buffer | pH: 8 |
Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI TALOS ARCTICA |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 46.6 e/Å2 |
Electron beam | Acceleration voltage: 200 kV / Electron source: ![]() |
Electron optics | Illumination mode: OTHER / Imaging mode: OTHER / Nominal defocus max: 2.2 µm / Nominal defocus min: 1.0 µm |
Experimental equipment | ![]() Model: Talos Arctica / Image courtesy: FEI Company |