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Yorodumi- EMDB-35333: Respiratory complex Membrane domain of CI, focus-refined of type ... -
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Open data
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Basic information
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| Title | Respiratory complex Membrane domain of CI, focus-refined of type IA, Wild type mouse under cold temperature | |||||||||
Map data | Focus-refined map, Membrane Domain, Cold Acclimated, Type IA of Respiratory Supercomplex | |||||||||
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Keywords | Respiratory complex / Respiratory supercomplex / ELECTRON TRANSPORT | |||||||||
| Function / homology | Function and homology informationMitochondrial protein import / Protein lipoylation / Mitochondrial Fatty Acid Beta-Oxidation / Complex I biogenesis / Respiratory electron transport / cellular response to oxygen levels / iron-sulfur cluster assembly complex / mitochondrial [2Fe-2S] 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 / iron-sulfur cluster assembly complex / mitochondrial [2Fe-2S] assembly complex / mitochondrial large ribosomal subunit binding / gliogenesis / negative regulation of non-canonical NF-kappaB signal transduction / positive regulation of mitochondrial membrane potential / neural precursor cell proliferation / [2Fe-2S] cluster assembly / oxygen sensor activity / iron-sulfur cluster assembly / NADH:ubiquinone reductase (H+-translocating) / positive regulation of ATP biosynthetic process / mitochondrial respiratory chain complex I assembly / proton motive force-driven mitochondrial ATP synthesis / mitochondrial electron transport, NADH to ubiquinone / respiratory chain complex I / NADH dehydrogenase (ubiquinone) activity / quinone binding / ATP synthesis coupled electron transport / negative regulation of reactive oxygen species biosynthetic process / neurogenesis / Neutrophil degranulation / reactive oxygen species metabolic process / aerobic respiration / cerebellum development / response to nicotine / response to cocaine / response to hydrogen peroxide / electron transport chain / 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 / structural molecule activity / mitochondrion / nucleoplasm / metal ion binding Similarity search - Function | |||||||||
| Biological species | ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.3 Å | |||||||||
Authors | Shin Y-C / Liao M | |||||||||
| Funding support | United States, 2 items
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Citation | Journal: Cell / Year: 2024Title: 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. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_35333.map.gz | 203.1 MB | EMDB map data format | |
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| Header (meta data) | emd-35333-v30.xml emd-35333.xml | 40.7 KB 40.7 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_35333_fsc.xml | 12.7 KB | Display | FSC data file |
| Images | emd_35333.png | 102.2 KB | ||
| Masks | emd_35333_msk_1.map | 216 MB | Mask map | |
| Filedesc metadata | emd-35333.cif.gz | 9.7 KB | ||
| Others | emd_35333_half_map_1.map.gz emd_35333_half_map_2.map.gz | 199 MB 199 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-35333 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-35333 | HTTPS FTP |
-Validation report
| Summary document | emd_35333_validation.pdf.gz | 1 MB | Display | EMDB validaton report |
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| Full document | emd_35333_full_validation.pdf.gz | 1 MB | Display | |
| Data in XML | emd_35333_validation.xml.gz | 21.7 KB | Display | |
| Data in CIF | emd_35333_validation.cif.gz | 28.2 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-35333 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-35333 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 8ib6MC ![]() 8iaoC ![]() 8iapC ![]() 8iaqC ![]() 8iarC ![]() 8ib4C ![]() 8ib5C ![]() 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 F&H Search |
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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_35333.map.gz / Format: CCP4 / Size: 216 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Annotation | Focus-refined map, Membrane Domain, Cold Acclimated, Type IA of Respiratory Supercomplex | ||||||||||||||||||||||||||||||||||||
| 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
| File | emd_35333_msk_1.map | ||||||||||||
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| Density Histograms |
-Half map: Focus-refined map, Membrane Domain, Cold Acclimated, Type IA...
| File | emd_35333_half_map_1.map | ||||||||||||
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| Annotation | Focus-refined map, Membrane Domain, Cold Acclimated, Type IA of Respiratory Supercomplex | ||||||||||||
| Projections & Slices |
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| Density Histograms |
-Half map: Focus-refined map, Membrane Domain, Cold Acclimated, Type IA...
| File | emd_35333_half_map_2.map | ||||||||||||
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| Annotation | Focus-refined map, Membrane Domain, Cold Acclimated, Type IA of Respiratory Supercomplex | ||||||||||||
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| Density Histograms |
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Sample components
+Entire : Respiratory Supercomplex CI:CIII2
+Supramolecule #1: Respiratory Supercomplex CI:CIII2
+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: ADENOSINE-5'-DIPHOSPHATE
+Macromolecule #28: ~{S}-[2-[3-[[(2~{R})-3,3-dimethyl-2-oxidanyl-4-phosphonooxy-butan...
-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 | 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 | #0 - Image recording ID: 1 / #0 - Film or detector model: GATAN K3 (6k x 4k) / #0 - Average electron dose: 46.1 e/Å2 / #1 - Image recording ID: 2 / #1 - Film or detector model: GATAN K3 (6k x 4k) / #1 - Average electron dose: 45.9 e/Å2 |
| Electron beam | Acceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN |
| 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 |
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About Yorodumi



Keywords
Authors
United States, 2 items
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Processing
FIELD EMISSION GUN

