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Yorodumi- EMDB-4479: CI Membrane Arm focused refinement from Ovine respiratory SC I+III2 -
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Open data
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Basic information
| Entry | Database: EMDB / ID: EMD-4479 | |||||||||
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| Title | CI Membrane Arm focused refinement from Ovine respiratory SC I+III2 | |||||||||
Map data | Focused refinement around CI membrane arm of ovine SC I III2. | |||||||||
Sample |
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Keywords | complex I / membrane arm / cellular respiration / mitochondria / ELECTRON TRANSPORT | |||||||||
| Function / homology | Function and homology information: / : / oxidoreductase activity, acting on NAD(P)H / acyl binding / ubiquinone binding / electron transport coupled proton transport / acyl carrier activity / NADH:ubiquinone reductase (H+-translocating) / mitochondrial respiratory chain complex I assembly / mitochondrial electron transport, NADH to ubiquinone ...: / : / oxidoreductase activity, acting on NAD(P)H / acyl binding / ubiquinone binding / electron transport coupled proton transport / acyl carrier activity / NADH:ubiquinone reductase (H+-translocating) / mitochondrial respiratory chain complex I assembly / mitochondrial electron transport, NADH to ubiquinone / respiratory chain complex I / membrane => GO:0016020 / NADH dehydrogenase (ubiquinone) activity / quinone binding / ATP synthesis coupled electron transport / reactive oxygen species metabolic process / electron transport chain / mitochondrial intermembrane space / NAD binding / 4 iron, 4 sulfur cluster binding / mitochondrial inner membrane / mitochondrial matrix / mitochondrion Similarity search - Function | |||||||||
| Biological species | ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.9 Å | |||||||||
Authors | Letts JA / Sazanov LA | |||||||||
| Funding support | Austria, 1 items
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Citation | Journal: Mol Cell / Year: 2019Title: Structures of Respiratory Supercomplex I+III Reveal Functional and Conformational Crosstalk. Authors: James A Letts / Karol Fiedorczuk / Gianluca Degliesposti / Mark Skehel / Leonid A Sazanov / ![]() Abstract: The mitochondrial electron transport chain complexes are organized into supercomplexes (SCs) of defined stoichiometry, which have been proposed to regulate electron flux via substrate channeling. We ...The mitochondrial electron transport chain complexes are organized into supercomplexes (SCs) of defined stoichiometry, which have been proposed to regulate electron flux via substrate channeling. We demonstrate that CoQ trapping in the isolated SC I+III limits complex (C)I turnover, arguing against channeling. The SC structure, resolved at up to 3.8 Å in four distinct states, suggests that CoQ oxidation may be rate limiting because of unequal access of CoQ to the active sites of CIII. CI shows a transition between "closed" and "open" conformations, accompanied by the striking rotation of a key transmembrane helix. Furthermore, the state of CI affects the conformational flexibility within CIII, demonstrating crosstalk between the enzymes. CoQ was identified at only three of the four binding sites in CIII, suggesting that interaction with CI disrupts CIII symmetry in a functionally relevant manner. Together, these observations indicate a more nuanced functional role for the SCs. | |||||||||
| History |
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Structure visualization
| Movie |
Movie viewer |
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| Structure viewer | EM map: SurfView Molmil Jmol/JSmol |
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_4479.map.gz | 479.6 MB | EMDB map data format | |
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| Header (meta data) | emd-4479-v30.xml emd-4479.xml | 52 KB 52 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_4479_fsc.xml | 18.1 KB | Display | FSC data file |
| Images | emd_4479.png | 53.6 KB | ||
| Masks | emd_4479_msk_1.map | 512 MB | Mask map | |
| Filedesc metadata | emd-4479.cif.gz | 11.4 KB | ||
| Others | emd_4479_half_map_1.map.gz emd_4479_half_map_2.map.gz | 410.6 MB 410.8 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-4479 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-4479 | HTTPS FTP |
-Validation report
| Summary document | emd_4479_validation.pdf.gz | 894.9 KB | Display | EMDB validaton report |
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| Full document | emd_4479_full_validation.pdf.gz | 894.5 KB | Display | |
| Data in XML | emd_4479_validation.xml.gz | 25.8 KB | Display | |
| Data in CIF | emd_4479_validation.cif.gz | 34.5 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-4479 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-4479 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 6q9bMC ![]() 4480C ![]() 4481C ![]() 4482C ![]() 4493C ![]() 4494C ![]() 4495C ![]() 4496C ![]() 4497C ![]() 4498C ![]() 4499C ![]() 4500C ![]() 4501C ![]() 4502C ![]() 4505C ![]() 4506C ![]() 4507C ![]() 6q9dC ![]() 6q9eC ![]() 6qa9C ![]() 6qbxC ![]() 6qc2C ![]() 6qc3C ![]() 6qc4C ![]() 6qc5C ![]() 6qc6C ![]() 6qc7C ![]() 6qc8C ![]() 6qc9C ![]() 6qcaC ![]() 6qcfC M: atomic model generated by this map C: citing same article ( |
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| Similar structure data |
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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_4479.map.gz / Format: CCP4 / Size: 512 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Annotation | Focused refinement around CI membrane arm of ovine SC I III2. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.4 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Mask #1
| File | emd_4479_msk_1.map | ||||||||||||
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| Projections & Slices |
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| Density Histograms |
-Half map: Focused refinement around CI membrane arm of ovine...
| File | emd_4479_half_map_1.map | ||||||||||||
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| Annotation | Focused refinement around CI membrane arm of ovine SC I III2. Half map 1 | ||||||||||||
| Projections & Slices |
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| Density Histograms |
-Half map: Focused refinement around CI membrane arm of ovine...
| File | emd_4479_half_map_2.map | ||||||||||||
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| Annotation | Focused refinement around CI membrane arm of ovine SC I III2. Half map 2 | ||||||||||||
| Projections & Slices |
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| Density Histograms |
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Sample components
+Entire : Ovine mitochondrial SC I+III2
+Supramolecule #1: Ovine mitochondrial SC I+III2
+Macromolecule #1: NADH:ubiquinone oxidoreductase core subunit S2,NADH:ubiquinone ox...
+Macromolecule #2: NADH-ubiquinone oxidoreductase chain 3
+Macromolecule #3: NADH-ubiquinone oxidoreductase chain 1
+Macromolecule #4: NADH-ubiquinone oxidoreductase chain 6
+Macromolecule #5: NADH-ubiquinone oxidoreductase chain 4L
+Macromolecule #6: NADH-ubiquinone oxidoreductase chain 5
+Macromolecule #7: NADH-ubiquinone oxidoreductase chain 4
+Macromolecule #8: NADH-ubiquinone oxidoreductase chain 2
+Macromolecule #9: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 11
+Macromolecule #10: NADH:ubiquinone oxidoreductase subunit B5
+Macromolecule #11: Acyl carrier protein
+Macromolecule #12: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8
+Macromolecule #13: NADH:ubiquinone oxidoreductase subunit B10
+Macromolecule #14: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mi...
+Macromolecule #15: NADH:ubiquinone oxidoreductase subunit S5
+Macromolecule #16: NADH:ubiquinone oxidoreductase subunit A3
+Macromolecule #17: NADH:ubiquinone oxidoreductase subunit B3
+Macromolecule #18: NADH dehydrogenase [ubiquinone] 1 subunit C2
+Macromolecule #19: NADH:ubiquinone oxidoreductase subunit B4
+Macromolecule #20: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13
+Macromolecule #21: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 6
+Macromolecule #22: NADH:ubiquinone oxidoreductase subunit B7
+Macromolecule #23: NADH:ubiquinone oxidoreductase subunit B9
+Macromolecule #24: NADH:ubiquinone oxidoreductase subunit B2
+Macromolecule #25: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mito...
+Macromolecule #26: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 11, mit...
+Macromolecule #27: NADH dehydrogenase [ubiquinone] 1 subunit C1, mitochondrial
+Macromolecule #28: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 1
+Macromolecule #29: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1
+Macromolecule #30: 1,2-Distearoyl-sn-glycerophosphoethanolamine
+Macromolecule #31: CARDIOLIPIN
+Macromolecule #32: 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE
+Macromolecule #33: S-[2-({N-[(2S)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-b...
-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 | 2 mg/mL | ||||||||||||
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| Buffer | pH: 7.4 Component:
Details: 250 mM NaCl, 20 mM HEPES, pH 7.7, 0.02% Brij-35 | ||||||||||||
| Grid | Model: Quantifoil R0.6/1 / Material: COPPER / Mesh: 300 / Support film - Material: CARBON / Support film - topology: HOLEY / Support film - Film thickness: 20 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 120 sec. / Pretreatment - Atmosphere: AIR / Pretreatment - Pressure: 0.067 kPa | ||||||||||||
| Vitrification | Cryogen name: PROPANE / Chamber humidity: 95 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV Details: blotting for 30 seconds at 4 degrees Celsius, 95% humidity and flash freezing. |
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Electron microscopy
| Microscope | FEI TITAN KRIOS |
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| Image recording | Film or detector model: FEI FALCON II (4k x 4k) / Number grids imaged: 1 / Number real images: 1854 / Average exposure time: 2.0 sec. / Average electron dose: 51.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: OTHER / Imaging mode: BRIGHT FIELD |
| Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi


Keywords
Authors
Austria, 1 items
Citation
UCSF Chimera









































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