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- EMDB-11875: Cryo-EM structure of Arabidopsis thaliana complex-I (open conform... -
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Open data
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Basic information
Entry | Database: EMDB / ID: EMD-11875 | |||||||||
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Title | Cryo-EM structure of Arabidopsis thaliana complex-I (open conformation) | |||||||||
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Function / homology | ![]() anther dehiscence / vegetative to reproductive phase transition of meristem / cold acclimation / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | |||||||||
Biological species | ![]() ![]() ![]() ![]() ![]() ![]() | |||||||||
Method | ![]() ![]() | |||||||||
![]() | Klusch N / Kuelbrandt W | |||||||||
Funding support | ![]()
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![]() | ![]() Title: A ferredoxin bridge connects the two arms of plant mitochondrial complex I. Authors: Niklas Klusch / Jennifer Senkler / Özkan Yildiz / Werner Kühlbrandt / Hans-Peter Braun / ![]() Abstract: Mitochondrial complex I is the main site for electron transfer to the respiratory chain and generates much of the proton gradient across the inner mitochondrial membrane. Complex I is composed of two ...Mitochondrial complex I is the main site for electron transfer to the respiratory chain and generates much of the proton gradient across the inner mitochondrial membrane. Complex I is composed of two arms, which form a conserved L-shape. We report the structures of the intact, 47-subunit mitochondrial complex I from Arabidopsis thaliana and the 51-subunit complex I from the green alga Polytomella sp., both at around 2.9 Å resolution. In both complexes, a heterotrimeric γ-carbonic anhydrase domain is attached to the membrane arm on the matrix side. Two states are resolved in A. thaliana complex I, with different angles between the two arms and different conformations of the ND1 (NADH dehydrogenase subunit 1) loop near the quinol binding site. The angle appears to depend on a bridge domain, which links the peripheral arm to the membrane arm and includes an unusual ferredoxin. We propose that the bridge domain participates in regulating the activity of plant complex I. | |||||||||
History |
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Structure visualization
Movie |
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Structure viewer | EM map: ![]() ![]() ![]() |
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 52.4 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 60.7 KB 60.7 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 21.3 KB | Display | ![]() |
Images | ![]() | 129.9 KB | ||
Others | ![]() ![]() | 672.4 MB 672.5 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7ar7MC ![]() 7aqqC ![]() 7aqrC ![]() 7aqwC ![]() 7ar8C ![]() 7ar9C ![]() 7arbC ![]() 7arcC ![]() 7ardC 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 | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
File | ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Voxel size | X=Y=Z: 0.837 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Half map: #2
File | emd_11875_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_11875_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
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Sample components
+Entire : Cryo-EM structure of Arabidopsis thaliana complex-I (open conform...
+Supramolecule #1: Cryo-EM structure of Arabidopsis thaliana complex-I (open conform...
+Macromolecule #1: NADH-ubiquinone oxidoreductase chain 3
+Macromolecule #2: NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial
+Macromolecule #3: NADH dehydrogenase [ubiquinone] iron-sulfur protein 3
+Macromolecule #4: NADH dehydrogenase [ubiquinone] iron-sulfur protein 2
+Macromolecule #5: NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial
+Macromolecule #6: NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial
+Macromolecule #7: NADH dehydrogenase [ubiquinone] iron-sulfur protein 1, mitochondrial
+Macromolecule #8: NADH-ubiquinone oxidoreductase chain 1
+Macromolecule #9: NADH dehydrogenase [ubiquinone] iron-sulfur protein 8-A, mitochondrial
+Macromolecule #10: NADH-ubiquinone oxidoreductase chain 6
+Macromolecule #11: NADH-ubiquinone oxidoreductase chain 4L
+Macromolecule #12: NADH-ubiquinone oxidoreductase chain 5
+Macromolecule #13: NADH-ubiquinone oxidoreductase chain 4
+Macromolecule #14: NADH-ubiquinone oxidoreductase chain 2
+Macromolecule #15: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mit...
+Macromolecule #16: NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial
+Macromolecule #17: NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial
+Macromolecule #18: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2
+Macromolecule #19: Acyl carrier protein 1, mitochondrial
+Macromolecule #20: Acyl carrier protein 2, mitochondrial
+Macromolecule #21: Probable NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subun...
+Macromolecule #22: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6
+Macromolecule #23: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8-B
+Macromolecule #24: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13-A
+Macromolecule #25: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1
+Macromolecule #26: At2g46540/F11C10.23
+Macromolecule #27: Transmembrane protein
+Macromolecule #28: Excitatory amino acid transporter
+Macromolecule #29: NADH dehydrogenase [ubiquinone] iron-sulfur protein 5-A
+Macromolecule #30: At4g16450
+Macromolecule #31: ESSS subunit of NADH:ubiquinone oxidoreductase (Complex I) protein
+Macromolecule #32: At1g67350
+Macromolecule #33: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 2
+Macromolecule #34: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3-A
+Macromolecule #35: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mito...
+Macromolecule #36: AT2G31490 protein
+Macromolecule #37: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9
+Macromolecule #38: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7
+Macromolecule #39: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10-B
+Macromolecule #40: Probable NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12
+Macromolecule #41: B14.5a
+Macromolecule #42: unknown
+Macromolecule #43: Uncharacterized protein At2g27730, mitochondrial
+Macromolecule #44: Gamma carbonic anhydrase-like 2, mitochondrial
+Macromolecule #45: Gamma carbonic anhydrase 2, mitochondrial
+Macromolecule #46: Gamma carbonic anhydrase 1, mitochondrial
+Macromolecule #47: IRON/SULFUR CLUSTER
+Macromolecule #48: FE2/S2 (INORGANIC) CLUSTER
+Macromolecule #49: FLAVIN MONONUCLEOTIDE
+Macromolecule #50: Ubiquinone-9
+Macromolecule #51: PHOSPHATIDYLETHANOLAMINE
+Macromolecule #52: (7S)-4-HYDROXY-N,N,N-TRIMETHYL-9-OXO-7-[(PALMITOYLOXY)METHYL]-3,5...
+Macromolecule #53: Lauryl Maltose Neopentyl Glycol
+Macromolecule #54: NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
+Macromolecule #55: ZINC ION
+Macromolecule #56: S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-b...
+Macromolecule #57: (1S)-2-{[{[(2R)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-...
+Macromolecule #58: 1,2-DICAPROYL-SN-PHOSPHATIDYL-L-SERINE
+Macromolecule #59: Phosphatidylinositol
-Experimental details
-Structure determination
Method | ![]() |
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Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.8 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD![]() |
Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 43.0 e/Å2 |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |