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Yorodumi- PDB-8ib9: Respiratory complex CI:CIII2, type IB, Wild type mouse under cold... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 8ib9 | |||||||||
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| Title | Respiratory complex CI:CIII2, type IB, Wild type mouse under cold temperature | |||||||||
Components |
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Keywords | ELECTRON TRANSPORT / Respiratory complex / Respiratory supercomplex | |||||||||
| Function / homology | Function and homology informationresponse to D-galactosamine / Complex III assembly / Mitochondrial protein import / response to injury involved in regulation of muscle adaptation / Protein lipoylation / Mitochondrial Fatty Acid Beta-Oxidation / Complex I biogenesis / RHOG GTPase cycle / response to mercury ion / subthalamus development ...response to D-galactosamine / Complex III assembly / Mitochondrial protein import / response to injury involved in regulation of muscle adaptation / Protein lipoylation / Mitochondrial Fatty Acid Beta-Oxidation / Complex I biogenesis / RHOG GTPase cycle / response to mercury ion / subthalamus development / pons development / Respiratory electron transport / protein insertion into mitochondrial inner membrane / response to cobalamin / cerebellar Purkinje cell layer development / blastocyst hatching / mitochondrial respiratory chain complex III assembly / pyramidal neuron development / respiratory system process / response to alkaloid / psychomotor behavior / cellular respiration / thalamus development / Mitochondrial protein degradation / cellular response to oxygen levels / response to light intensity / mesenchymal stem cell proliferation / respiratory chain complex / reproductive system development / mitochondrial [2Fe-2S] assembly complex / iron-sulfur cluster assembly complex / mitochondrial large ribosomal subunit binding / gliogenesis / mesenchymal stem cell differentiation / circulatory system development / respiratory chain complex III / negative regulation of non-canonical NF-kappaB signal transduction / cardiac muscle tissue development / quinol-cytochrome-c reductase / neural precursor cell proliferation / [2Fe-2S] cluster assembly / response to glucagon / adult walking behavior / oxygen sensor activity / positive regulation of mitochondrial membrane potential / response to hydroperoxide / quinol-cytochrome-c reductase activity / cellular response to glucocorticoid stimulus / stem cell division / response to copper ion / mitochondrial electron transport, ubiquinol to cytochrome c / NADH dehydrogenase activity / iron-sulfur cluster assembly / hypothalamus development / midbrain development / electron transport coupled proton transport / dopamine metabolic process / mitochondrial ATP synthesis coupled electron transport / NADH:ubiquinone reductase (H+-translocating) / adult behavior / positive regulation of ATP biosynthetic process / mitochondrial respiratory chain complex I assembly / mitochondrial electron transport, NADH to ubiquinone / proton motive force-driven mitochondrial ATP synthesis / respiratory chain complex I / positive regulation of execution phase of apoptosis / animal organ regeneration / response to hyperoxia / NADH dehydrogenase (ubiquinone) activity / response to cadmium ion / neuron development / quinone binding / cellular response to interferon-beta / ATP synthesis coupled electron transport / response to hormone / negative regulation of reactive oxygen species biosynthetic process / extrinsic apoptotic signaling pathway / cellular response to retinoic acid / tricarboxylic acid cycle / neurogenesis / Neutrophil degranulation / visual perception / muscle contraction / reactive oxygen species metabolic process / aerobic respiration / cerebellum development / response to activity / regulation of mitochondrial membrane potential / respiratory electron transport chain / response to nicotine / response to cocaine / mitochondrion organization / hippocampus development / DNA damage response, signal transduction by p53 class mediator / kidney development / response to hydrogen peroxide / monooxygenase activity / sensory perception of sound / fatty acid metabolic process / electron transport chain Similarity search - Function | |||||||||
| Biological species | ![]() | |||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4.3 Å | |||||||||
Authors | Shin, Y.-C. / Liao, M. | |||||||||
| Funding support | United States, 2items
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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. | |||||||||
| History |
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 8ib9.cif.gz | 2.2 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb8ib9.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 8ib9.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 8ib9_validation.pdf.gz | 4.2 MB | Display | wwPDB validaton report |
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| Full document | 8ib9_full_validation.pdf.gz | 4.4 MB | Display | |
| Data in XML | 8ib9_validation.xml.gz | 307 KB | Display | |
| Data in CIF | 8ib9_validation.cif.gz | 467.5 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ib/8ib9 ftp://data.pdbj.org/pub/pdb/validation_reports/ib/8ib9 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 35336MC ![]() 8iaoC ![]() 8iapC ![]() 8iaqC ![]() 8iarC ![]() 8ib4C ![]() 8ib5C ![]() 8ib6C ![]() 8ib7C ![]() 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: map data used to model this data C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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Components
-NADH-ubiquinone oxidoreductase chain ... , 7 types, 7 molecules AHJKLMN
| #1: Protein | Mass: 13223.775 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() References: UniProt: P03899, NADH:ubiquinone reductase (H+-translocating) |
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| #8: Protein | Mass: 36077.016 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() References: UniProt: P03888, NADH:ubiquinone reductase (H+-translocating) |
| #10: Protein | Mass: 18628.090 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() References: UniProt: P03925, NADH:ubiquinone reductase (H+-translocating) |
| #11: Protein | Mass: 10609.619 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() References: UniProt: P03903, NADH:ubiquinone reductase (H+-translocating) |
| #12: Protein | Mass: 68519.289 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() References: UniProt: P03921, NADH:ubiquinone reductase (H+-translocating) |
| #13: Protein | Mass: 51915.535 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() References: UniProt: P03911, NADH:ubiquinone reductase (H+-translocating) |
| #14: Protein | Mass: 38772.219 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() References: UniProt: P03893, NADH:ubiquinone reductase (H+-translocating) |
-NADH dehydrogenase [ubiquinone] iron-sulfur protein ... , 7 types, 7 molecules BCDIQRe
| #2: Protein | Mass: 24715.912 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() References: UniProt: Q9DC70, NADH:ubiquinone reductase (H+-translocating) |
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| #3: Protein | Mass: 30191.307 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() References: UniProt: Q9DCT2, NADH:ubiquinone reductase (H+-translocating) |
| #4: Protein | Mass: 52693.559 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() References: UniProt: Q91WD5, NADH:ubiquinone reductase (H+-translocating) |
| #9: Protein | Mass: 24068.355 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() References: UniProt: Q8K3J1, NADH:ubiquinone reductase (H+-translocating) |
| #17: Protein | Mass: 19814.725 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #18: Protein | Mass: 13041.828 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #30: Protein | Mass: 12675.772 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-NADH dehydrogenase [ubiquinone] flavoprotein ... , 3 types, 3 molecules EFs
| #5: Protein | Mass: 27318.336 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() References: UniProt: Q9D6J6, NADH:ubiquinone reductase (H+-translocating) |
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| #6: Protein | Mass: 50904.152 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() References: UniProt: Q91YT0, NADH:ubiquinone reductase (H+-translocating) |
| #44: Protein | Mass: 11833.504 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Protein , 4 types, 7 molecules GTUACAcADAd
| #7: Protein | Mass: 79866.688 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() References: UniProt: Q91VD9, NADH:ubiquinone reductase (H+-translocating) | ||||
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| #20: Protein | Mass: 17390.289 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #47: Protein | Mass: 43240.305 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #48: Protein | Mass: 35374.652 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() |
-NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit ... , 12 types, 12 molecules OPSVWXYZabqr
| #15: Protein | Mass: 40657.375 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #16: Protein | Mass: 42588.129 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #19: Protein | Mass: 10932.675 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #21: Protein | Mass: 13380.719 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #22: Protein | Mass: 15311.858 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #23: Protein | Mass: 20025.127 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #24: Protein | Mass: 15130.416 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #25: Protein | Mass: 16881.588 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #26: Protein | Mass: 8149.524 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #27: Protein | Mass: 9338.867 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #42: Protein | Mass: 17112.416 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #43: Protein | Mass: 12595.592 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-NADH dehydrogenase [ubiquinone] 1 subunit ... , 2 types, 2 molecules cd
| #28: Protein | Mass: 8636.023 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #29: Protein | Mass: 14185.692 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit ... , 11 types, 11 molecules fghijklmnop
| #31: Protein | Mass: 6965.109 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #32: Protein | Mass: 17463.727 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #33: Protein | Mass: 21742.197 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #34: Protein | Mass: 15540.085 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #35: Protein | Mass: 11982.437 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #36: Protein | Mass: 11714.240 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #37: Protein | Mass: 21903.828 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #38: Protein | Mass: 15105.287 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #39: Protein | Mass: 22020.123 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #40: Protein | Mass: 16360.804 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #41: Protein | Mass: 21054.832 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Cytochrome b-c1 complex subunit ... , 8 types, 17 molecules AAAaABAbAEAIAeAFAfAGAgAHAhAJAjAKAk
| #45: Protein | Mass: 52910.594 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #46: Protein | Mass: 48289.730 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #49: Protein | Mass: 29406.635 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) ![]() #50: Protein | Mass: 13587.532 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #51: Protein | Mass: 9783.245 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #52: Protein | Mass: 10452.694 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #53: Protein | Mass: 7457.526 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #54: Protein | Mass: 6546.627 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-Non-polymers , 16 types, 55 molecules 






























| #55: Chemical | ChemComp-SF4 / #56: Chemical | ChemComp-UQ1 / | #57: Chemical | #58: Chemical | ChemComp-3PE / #59: Chemical | #60: Chemical | ChemComp-FMN / | #61: Chemical | ChemComp-UQ9 / | #62: Chemical | ChemComp-CDL / #63: Chemical | ChemComp-ADP / | #64: Chemical | ChemComp-NDP / | #65: Chemical | ChemComp-ZN / | #66: Chemical | #67: Chemical | ChemComp-HEM / #68: Chemical | #69: Chemical | #70: Chemical | |
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-Details
| Has ligand of interest | Y |
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| Has protein modification | Y |
-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
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| EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
| Component | Name: Respiratory Supercomplex CI:CIII2 / Type: COMPLEX / Entity ID: #1-#54 / Source: NATURAL |
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| Molecular weight | Value: 1.32 MDa / Experimental value: NO |
| Source (natural) | Organism: ![]() |
| Buffer solution | pH: 8 |
| Specimen | Conc.: 0.33 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Talos Arctica / Image courtesy: FEI Company | ||||||||||||
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| Microscopy | Model: FEI TALOS ARCTICA | ||||||||||||
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 200 kV / Illumination mode: OTHER | ||||||||||||
| Electron lens | Mode: OTHER / Nominal defocus max: 2200 nm / Nominal defocus min: 1000 nm | ||||||||||||
| Image recording |
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Processing
| CTF correction | Type: NONE |
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| 3D reconstruction | Resolution: 4.3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 37608 / Symmetry type: POINT |
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United States, 2items
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FIELD EMISSION GUN