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Yorodumi- EMDB-35315: Respiratory complex Membrane domain of CI, focused map of type I,... -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-35315 | |||||||||
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Title | Respiratory complex Membrane domain of CI, focused map of type I, Wild type mouse under thermoneutral temperature | |||||||||
Map data | Focus-refined map, Membrane Domain, Thermoneutral, Type I of Respiratory Supercomplex CI:CIII2 | |||||||||
Sample |
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Keywords | Respiratory complex / Respiratory supercomplex / ELECTRON TRANSPORT | |||||||||
Function / homology | Function and homology information 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 large ribosomal subunit binding / gliogenesis / negative regulation of non-canonical NF-kappaB signal transduction ...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 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 / : / ubiquinone binding / iron-sulfur cluster assembly / positive regulation of ATP biosynthetic process / NADH:ubiquinone reductase (H+-translocating) / proton motive force-driven mitochondrial ATP synthesis / NADH dehydrogenase activity / mitochondrial ATP synthesis coupled electron transport / : / mitochondrial respiratory chain complex I assembly / mitochondrial electron transport, NADH to ubiquinone / electron transport coupled proton transport / respiratory chain complex I / acyl binding / acyl carrier activity / NADH dehydrogenase (ubiquinone) activity / ATP synthesis coupled electron transport / quinone binding / negative regulation of reactive oxygen species biosynthetic process / ionotropic glutamate receptor binding / Neutrophil degranulation / aerobic respiration / cerebellum development / reactive oxygen species metabolic process / neurogenesis / response to cocaine / response to nicotine / electron transport chain / response to hydrogen peroxide / mitochondrial intermembrane space / NAD binding / myelin sheath / 4 iron, 4 sulfur cluster binding / response to ethanol / in utero embryonic development / response to oxidative stress / mitochondrial inner membrane / response to hypoxia / nuclear speck / mitochondrial matrix / ubiquitin protein ligase binding / protein-containing complex binding / protein kinase binding / endoplasmic reticulum / mitochondrion / nucleoplasm / metal ion binding / cytoplasm Similarity search - Function | |||||||||
Biological species | Mus musculus (house mouse) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.4 Å | |||||||||
Authors | Shin Y-C / Liao M | |||||||||
Funding support | United States, 2 items
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Citation | Journal: Cell / Year: 2024 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 | emd_35315.map.gz | 197.2 MB | EMDB map data format | |
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Header (meta data) | emd-35315-v30.xml emd-35315.xml | 40.7 KB 40.7 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_35315_fsc.xml | 12.7 KB | Display | FSC data file |
Images | emd_35315.png | 104.7 KB | ||
Masks | emd_35315_msk_1.map | 216 MB | Mask map | |
Filedesc metadata | emd-35315.cif.gz | 9.7 KB | ||
Others | emd_35315_half_map_1.map.gz emd_35315_half_map_2.map.gz | 193.7 MB 193.7 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-35315 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-35315 | HTTPS FTP |
-Validation report
Summary document | emd_35315_validation.pdf.gz | 1.1 MB | Display | EMDB validaton report |
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Full document | emd_35315_full_validation.pdf.gz | 1.1 MB | Display | |
Data in XML | emd_35315_validation.xml.gz | 21.6 KB | Display | |
Data in CIF | emd_35315_validation.cif.gz | 28.1 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-35315 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-35315 | HTTPS FTP |
-Related structure data
Related structure data | 8iaqMC 8iaoC 8iapC 8iarC 8ib4C 8ib5C 8ib6C 8ib7C 8ib9C 8ibaC 8ibbC 8ibcC 8ibdC 8ibeC 8ibfC 8ibgC 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 (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_35315.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, 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
File | emd_35315_msk_1.map | ||||||||||||
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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 |
-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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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Concentration | 0.33 mg/mL |
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Buffer | pH: 8 |
Vitrification | Cryogen name: ETHANE |
-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: 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 |