[English] 日本語

- EMDB-4480: CI Peripheral Arm focused refinement from Ovine respiratory SC I+III2 -
+
Open data
-
Basic information
Entry | Database: EMDB / ID: EMD-4480 | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Title | CI Peripheral Arm focused refinement from Ovine respiratory SC I+III2 | |||||||||
![]() | Focused refinement around complex I peripheral arm | |||||||||
![]() |
| |||||||||
![]() | complex I / peripheral arm / cellular respiration / mitochondria / ELECTRON TRANSPORT | |||||||||
Function / homology | ![]() : / : / apoptotic mitochondrial changes / acyl binding / acyl carrier activity / NADH:ubiquinone reductase (H+-translocating) / NADH dehydrogenase activity / mitochondrial electron transport, NADH to ubiquinone / mitochondrial respiratory chain complex I assembly / respiratory chain complex I ...: / : / apoptotic mitochondrial changes / acyl binding / acyl carrier activity / NADH:ubiquinone reductase (H+-translocating) / NADH dehydrogenase activity / mitochondrial electron transport, NADH to ubiquinone / mitochondrial respiratory chain complex I assembly / respiratory chain complex I / NADH dehydrogenase (ubiquinone) activity / ATP metabolic process / reactive oxygen species metabolic process / regulation of mitochondrial membrane potential / respiratory electron transport chain / electron transport chain / mitochondrial intermembrane space / 2 iron, 2 sulfur cluster binding / circadian rhythm / NAD binding / FMN binding / 4 iron, 4 sulfur cluster binding / response to oxidative stress / mitochondrial inner membrane / mitochondrial matrix / protein-containing complex binding / mitochondrion / metal ion binding Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.8 Å | |||||||||
![]() | Letts JA / Sazanov LA | |||||||||
Funding support | ![]()
| |||||||||
![]() | ![]() Title: 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 |
|
-
Structure visualization
Movie |
![]() |
---|---|
Structure viewer | EM map: ![]() ![]() ![]() |
Supplemental images |
-
Downloads & links
-EMDB archive
Map data | ![]() | 228.8 MB | ![]() | |
---|---|---|---|---|
Header (meta data) | ![]() ![]() | 39.2 KB 39.2 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 14.1 KB | Display | ![]() |
Images | ![]() | 63.9 KB | ||
Masks | ![]() | 244.1 MB | ![]() | |
Filedesc metadata | ![]() | 9.9 KB | ||
Others | ![]() ![]() | 194.7 MB 194.7 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 823 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 822.5 KB | Display | |
Data in XML | ![]() | 20.1 KB | Display | |
Data in CIF | ![]() | 27.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6q9dMC ![]() 4479C ![]() 4481C ![]() 4482C ![]() 4493C ![]() 4494C ![]() 4495C ![]() 4496C ![]() 4497C ![]() 4498C ![]() 4499C ![]() 4500C ![]() 4501C ![]() 4502C ![]() 4505C ![]() 4506C ![]() 4507C ![]() 6q9bC ![]() 6q9eC ![]() 6qa9C ![]() 6qbxC ![]() 6qc2C ![]() 6qc3C ![]() 6qc4C ![]() 6qc5C ![]() 6qc6C ![]() 6qc7C ![]() 6qc8C ![]() 6qc9C ![]() 6qcaC ![]() 6qcfC C: citing same article ( M: atomic model generated by this map |
---|---|
Similar structure data |
-
Links
EMDB pages | ![]() ![]() |
---|---|
Related items in Molecule of the Month |
-
Map
File | ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Annotation | Focused refinement around complex I peripheral arm | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.4 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
|
-Supplemental data
-Mask #1
File | ![]() | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Projections & Slices |
| ||||||||||||
Density Histograms |
-Half map: Focused refinement around complex I peripheral arm. Half map 1
File | emd_4480_half_map_1.map | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Annotation | Focused refinement around complex I peripheral arm. Half map 1 | ||||||||||||
Projections & Slices |
| ||||||||||||
Density Histograms |
-Half map: Focused refinement around complex I peripheral arm. Half map 2
File | emd_4480_half_map_2.map | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Annotation | Focused refinement around complex I peripheral arm. Half map 2 | ||||||||||||
Projections & Slices |
| ||||||||||||
Density Histograms |
-
Sample components
+Entire : Ovine mitochondrial SC I+III2
+Supramolecule #1: Ovine mitochondrial SC I+III2
+Macromolecule #1: NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial
+Macromolecule #2: NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial
+Macromolecule #3: NADH:ubiquinone oxidoreductase core subunit S1
+Macromolecule #4: NADH:ubiquinone oxidoreductase core subunit S2,NADH:ubiquinone ox...
+Macromolecule #5: NADH:ubiquinone oxidoreductase core subunit S3
+Macromolecule #6: NADH:ubiquinone oxidoreductase core subunit S7
+Macromolecule #7: NADH:ubiquinone oxidoreductase core subunit S8
+Macromolecule #8: NADH:ubiquinone oxidoreductase subunit V3
+Macromolecule #9: NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial
+Macromolecule #10: NADH:ubiquinone oxidoreductase subunit S4
+Macromolecule #11: NADH:ubiquinone oxidoreductase subunit A9
+Macromolecule #12: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2
+Macromolecule #13: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5
+Macromolecule #14: NADH:ubiquinone oxidoreductase subunit A6
+Macromolecule #15: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7
+Macromolecule #16: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12
+Macromolecule #17: Acyl carrier protein
+Macromolecule #18: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13
+Macromolecule #19: IRON/SULFUR CLUSTER
+Macromolecule #20: FLAVIN MONONUCLEOTIDE
+Macromolecule #21: FE2/S2 (INORGANIC) CLUSTER
+Macromolecule #22: ZINC ION
+Macromolecule #23: NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
+Macromolecule #24: S-[2-({N-[(2S)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-b...
-Experimental details
-Structure determination
Method | cryo EM |
---|---|
![]() | single particle reconstruction |
Aggregation state | particle |
-
Sample preparation
Concentration | 2 mg/mL | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Buffer | pH: 7.4 Component:
Details: 250 mM NaCl, 20 mM HEPES, pH 7.7, 0.02% Brij-35 | ||||||||||||
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. |
-
Electron microscopy
Microscope | FEI TITAN KRIOS |
---|---|
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: ![]() |
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 |