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- PDB-7ar7: Cryo-EM structure of Arabidopsis thaliana complex-I (open conform... -
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Open data
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Basic information
Entry | Database: PDB / ID: 7ar7 | ||||||
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Title | Cryo-EM structure of Arabidopsis thaliana complex-I (open conformation) | ||||||
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![]() | ELECTRON TRANSPORT / Complex-I Arabidopsis | ||||||
Function / homology | ![]() anther dehiscence / vegetative to reproductive phase transition of meristem / cold acclimation / Lyases; Carbon-oxygen lyases; Hydro-lyases / : / photorespiration / embryo development ending in seed dormancy / NADH dehydrogenase complex / response to abscisic acid / plant-type vacuole ...anther dehiscence / vegetative to reproductive phase transition of meristem / cold acclimation / Lyases; Carbon-oxygen lyases; Hydro-lyases / : / photorespiration / embryo development ending in seed dormancy / NADH dehydrogenase complex / response to abscisic acid / plant-type vacuole / cobalt ion binding / response to osmotic stress / regulation of reactive oxygen species metabolic process / plastid / protein homotrimerization / ubiquinone binding / acyl carrier activity / electron transport coupled proton transport / NADH:ubiquinone reductase (H+-translocating) / mitochondrial electron transport, NADH to ubiquinone / respiratory chain complex I / NADH dehydrogenase (ubiquinone) activity / quinone binding / ATP synthesis coupled electron transport / response to salt stress / proton transmembrane transport / aerobic respiration / chloroplast / respiratory electron transport chain / carbonate dehydratase activity / electron transport chain / mitochondrial membrane / mitochondrial intermembrane space / 2 iron, 2 sulfur cluster binding / NAD binding / fatty acid biosynthetic process / peroxisome / FMN binding / 4 iron, 4 sulfur cluster binding / carbohydrate metabolic process / mitochondrial inner membrane / mitochondrial matrix / copper ion binding / nucleolus / mitochondrion / extracellular region / zinc ion binding / metal ion binding / identical protein binding / nucleus / membrane / plasma membrane / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.72 Å | ||||||
![]() | 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 | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 1.3 MB | Display | ![]() |
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PDB format | ![]() | 1.1 MB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 11875MC ![]() 7aqqC ![]() 7aqrC ![]() 7aqwC ![]() 7ar8C ![]() 7ar9C ![]() 7arbC ![]() 7arcC ![]() 7ardC M: map data used to model this data C: citing same article ( |
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Similar structure data |
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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
+NADH dehydrogenase [ubiquinone] iron-sulfur protein ... , 8 types, 8 molecules BCDGIQRe
+NADH dehydrogenase [ubiquinone] flavoprotein ... , 2 types, 2 molecules EF
+NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit ... , 6 types, 6 molecules PSWXZa
+Acyl carrier protein ... , 2 types, 2 molecules TU
+Probable NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit ... , 2 types, 2 molecules Vq
+Protein/peptide , 4 types, 4 molecules bruv
+Protein , 7 types, 7 molecules cdfgimx
+NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit ... , 6 types, 6 molecules jklnop
+Gamma carbonic anhydrase ... , 2 types, 2 molecules yz
+Non-polymers , 13 types, 24 molecules 
























+Details
-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: Cryo-EM structure of Arabidopsis thaliana complex-I (open conformation) Type: COMPLEX / Entity ID: #1-#46 / Source: NATURAL |
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Source (natural) | Organism: ![]() ![]() |
Buffer solution | pH: 7.8 |
Specimen | 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: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: ![]() |
Electron lens | Mode: BRIGHT FIELD |
Image recording | Electron dose: 43 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
Software | Name: PHENIX / Version: 1.19.2_4158: / Classification: refinement | ||||||||||||||||||||||||
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
3D reconstruction | Resolution: 3.72 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 48933 / Symmetry type: POINT | ||||||||||||||||||||||||
Refine LS restraints |
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