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Yorodumi- PDB-9ti4: High resolution Cryo-EM structure of human complex I in mitochondria -
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Open data
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Basic information
| Entry | Database: PDB / ID: 9ti4 | ||||||
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| Title | High resolution Cryo-EM structure of human complex I in mitochondria | ||||||
Components |
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Keywords | MEMBRANE PROTEIN / Human mitochondria / respirasome complex / complex I / NADH dehydrogenase | ||||||
| Function / homology | Function and homology informationComplex I biogenesis / protein lipoylation / Mitochondrial Fatty Acid Beta-Oxidation / Protein lipoylation / Respiratory electron transport / protein insertion into mitochondrial inner membrane / ubiquinone biosynthetic process / blastocyst hatching / cellular respiration / response to light intensity ...Complex I biogenesis / protein lipoylation / Mitochondrial Fatty Acid Beta-Oxidation / Protein lipoylation / Respiratory electron transport / protein insertion into mitochondrial inner membrane / ubiquinone biosynthetic process / blastocyst hatching / cellular respiration / response to light intensity / cellular response to oxygen levels / Mitochondrial protein import / iron-sulfur cluster assembly complex / mesenchymal stem cell proliferation / reproductive system development / mitochondrial large ribosomal subunit binding / respiratory chain complex / gliogenesis / mitochondrial [2Fe-2S] assembly complex / oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor / mesenchymal stem cell differentiation / circulatory system development / negative regulation of non-canonical NF-kappaB signal transduction / cardiac muscle tissue development / positive regulation of mitochondrial membrane potential / response to hydroperoxide / neural precursor cell proliferation / [2Fe-2S] cluster assembly / oxygen sensor activity / cellular response to glucocorticoid stimulus / azurophil granule membrane / stem cell division / NADH dehydrogenase activity / iron-sulfur cluster assembly / sodium ion transport / ubiquinone binding / electron transport coupled proton transport / acyl binding / regulation of protein phosphorylation / NADH:ubiquinone reductase (H+-translocating) / acyl carrier activity / mitochondrial ATP synthesis coupled electron transport / 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 / RHOG GTPase cycle / respiratory chain complex I / positive regulation of execution phase of apoptosis / response to cAMP / NADH dehydrogenase (ubiquinone) activity / endopeptidase activator activity / quinone binding / cellular response to interferon-beta / negative regulation of reactive oxygen species biosynthetic process / extrinsic apoptotic signaling pathway / cellular response to retinoic acid / neurogenesis / ionotropic glutamate receptor binding / substantia nigra development / Mitochondrial protein degradation / reactive oxygen species metabolic process / muscle contraction / synaptic membrane / aerobic respiration / fatty acid binding / cerebellum development / regulation of mitochondrial membrane potential / respiratory electron transport chain / response to nicotine / DNA damage response, signal transduction by p53 class mediator / kidney development / monooxygenase activity / response to hydrogen peroxide / sensory perception of sound / fatty acid metabolic process / circadian rhythm / brain development / mitochondrial intermembrane space / 2 iron, 2 sulfur cluster binding / mitochondrial membrane / multicellular organism growth / NAD binding / fatty acid biosynthetic process / positive regulation of protein catabolic process / cellular senescence / FMN binding / nervous system development / 4 iron, 4 sulfur cluster binding / response to oxidative stress / protease binding / response to ethanol / gene expression / in utero embryonic development / response to hypoxia / electron transfer activity / mitochondrial inner membrane / nuclear speck / nuclear body / mitochondrial matrix Similarity search - Function | ||||||
| Biological species | Homo sapiens (human) | ||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.66 Å | ||||||
Authors | Nguyen, M.D. / Singh, V. / Rorbach, J. | ||||||
| Funding support | Sweden, 1items
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Citation | Journal: To Be PublishedTitle: Structural basis for late maturation steps of mitochondrial respiratory chain complex IV within the human respirasome Authors: Nguyen, M.D. / Singh, V. / Rorbach, J. | ||||||
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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 | 9ti4.cif.gz | 3.1 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9ti4.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9ti4.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 9ti4_validation.pdf.gz | 3 MB | Display | wwPDB validaton report |
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| Full document | 9ti4_full_validation.pdf.gz | 3.1 MB | Display | |
| Data in XML | 9ti4_validation.xml.gz | 216.5 KB | Display | |
| Data in CIF | 9ti4_validation.cif.gz | 327.7 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ti/9ti4 ftp://data.pdbj.org/pub/pdb/validation_reports/ti/9ti4 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 54784MC ![]() 9hzlC ![]() 9i4iC ![]() 9i6fC ![]() 9i7uC C: citing same article ( M: map data used to model this data |
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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 dehydrogenase [ubiquinone] flavoprotein ... , 3 types, 3 molecules CKO
| #1: Protein | Mass: 47680.340 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human)References: UniProt: P49821, NADH:ubiquinone reductase (H+-translocating) |
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| #9: Protein/peptide | Mass: 4623.078 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P56181 |
| #13: Protein | Mass: 23430.881 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human)References: UniProt: P19404, NADH:ubiquinone reductase (H+-translocating) |
-NADH dehydrogenase [ubiquinone] iron-sulfur protein ... , 7 types, 7 molecules DELPQTh
| #2: Protein | Mass: 20314.037 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human)References: UniProt: O00217, NADH:ubiquinone reductase (H+-translocating) |
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| #3: Protein | Mass: 18449.473 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human)References: UniProt: O75251, NADH:ubiquinone reductase (H+-translocating) |
| #10: Protein | Mass: 14064.931 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O43181 |
| #14: Protein | Mass: 24432.656 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human)References: UniProt: O75489, NADH:ubiquinone reductase (H+-translocating) |
| #15: Protein | Mass: 49249.500 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human)References: UniProt: O75306, NADH:ubiquinone reductase (H+-translocating) |
| #17: Protein | Mass: 10716.994 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O75380 |
| #30: Protein | Mass: 12445.448 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O43920 |
-NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit ... , 12 types, 12 molecules FGIJNSUVWuwt
| #4: Protein | Mass: 14205.511 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P56556 |
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| #5: Protein | Mass: 9722.138 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O43678 |
| #7: Protein | Mass: 13119.208 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q16718 |
| #8: Protein | Mass: 38848.113 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q16795 |
| #12: Protein | Mass: 17011.266 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9UI09 |
| #16: Protein | Mass: 8084.391 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O15239 |
| #18: Protein | Mass: 9156.602 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O95167 |
| #19: Protein | Mass: 14736.853 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q86Y39 |
| #20: Protein | Mass: 16360.880 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9P0J0 |
| #41: Protein | Mass: 20007.902 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P51970 |
| #43: Protein | Mass: 37200.270 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O95299 |
| #44: Protein | Mass: 12571.403 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O95182 |
-Protein , 2 types, 3 molecules HXM
| #6: Protein | Mass: 9976.442 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O14561#11: Protein | | Mass: 75471.484 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human)References: UniProt: P28331, NADH:ubiquinone reductase (H+-translocating) |
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-NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit ... , 11 types, 11 molecules YZabcdenopv
| #21: Protein | Mass: 7624.451 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O95178 |
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| #22: Protein | Mass: 9575.944 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O43676 |
| #23: Protein | Mass: 16573.160 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O43674 |
| #24: Protein | Mass: 14491.033 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O95139 |
| #25: Protein | Mass: 18094.416 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O95169 |
| #26: Protein | Mass: 20489.350 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O96000 |
| #27: Protein | Mass: 12590.146 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9NX14 |
| #36: Protein | Mass: 6514.623 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O75438 |
| #37: Protein | Mass: 15100.399 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O95168 |
| #38: Protein | Mass: 21246.193 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9Y6M9 |
| #42: Protein | Mass: 14854.193 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P17568 |
-NADH dehydrogenase [ubiquinone] 1 subunit ... , 2 types, 2 molecules fg
| #28: Protein/peptide | Mass: 5904.838 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O43677 |
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| #29: Protein | Mass: 14209.521 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O95298 |
-NADH-ubiquinone oxidoreductase chain ... , 7 types, 7 molecules ijklmrs
| #31: Protein | Mass: 38980.633 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human)References: UniProt: P03891, NADH:ubiquinone reductase (H+-translocating) |
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| #32: Protein | Mass: 13189.951 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human)References: UniProt: P03897, NADH:ubiquinone reductase (H+-translocating) |
| #33: Protein | Mass: 10745.110 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human)References: UniProt: P03901, NADH:ubiquinone reductase (H+-translocating) |
| #34: Protein | Mass: 66836.633 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human)References: UniProt: P03915, NADH:ubiquinone reductase (H+-translocating) |
| #35: Protein | Mass: 18512.859 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human)References: UniProt: P03923, NADH:ubiquinone reductase (H+-translocating) |
| #39: Protein | Mass: 51613.547 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human)References: UniProt: P03905, NADH:ubiquinone reductase (H+-translocating) |
| #40: Protein | Mass: 35447.957 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human)References: UniProt: P03886, NADH:ubiquinone reductase (H+-translocating) |
-Non-polymers , 12 types, 36 molecules 






















| #45: Chemical | ChemComp-SF4 / #46: Chemical | ChemComp-FMN / | #47: Chemical | ChemComp-PEE / #48: Chemical | #49: Chemical | ChemComp-NDP / | #50: Chemical | #51: Chemical | ChemComp-PLX / ( #52: Chemical | ChemComp-ZN / | #53: Chemical | ChemComp-CDL / #54: Chemical | ChemComp-DGT / | #55: Chemical | ChemComp-MG / | #56: Water | ChemComp-HOH / | |
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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: NADH-ubiquinone oxidoreductase / Type: COMPLEX / Entity ID: #1-#44 / Source: NATURAL |
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| Molecular weight | Experimental value: NO |
| Source (natural) | Organism: Homo sapiens (human) |
| Buffer solution | pH: 7.4 Details: 25 mM HEPES-KOH pH=7.5, 50 mM KCl, 20 mM Mg(OAc)2, 0.01% (v/v) Lauryl Maltose Neopentyl Glycol (LMNG), 0.001 % cardiolipin, 0.001 % glycol-diosgenin (GDN, Sigma-Aldrich), 0.1mM DTT |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Specimen support | Grid material: COPPER / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil R2/2 |
| Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277 K |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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| Microscopy | Model: TFS KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: OTHER |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2000 nm / Nominal defocus min: 600 nm |
| Specimen holder | Cryogen: NITROGEN |
| Image recording | Electron dose: 35 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||
| Particle selection | Num. of particles selected: 2508182 | ||||||||||||||||
| 3D reconstruction | Resolution: 2.66 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 236346 / Symmetry type: POINT | ||||||||||||||||
| Atomic model building | Protocol: RIGID BODY FIT |
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Homo sapiens (human)
Sweden, 1items
Citation












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FIELD EMISSION GUN