+Open data
-Basic information
Entry | Database: PDB / ID: 6nby | ||||||||||||
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Title | T.elongatus NDH (composite model) | ||||||||||||
Components |
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Keywords | OXIDOREDUCTASE / photosynthesis / bioenergetics / membrane protein complex | ||||||||||||
Function / homology | Function and homology information : / Translocases; Catalysing the translocation of protons; Linked to oxidoreductase reactions / photosynthetic electron transport chain / oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor / NADH dehydrogenase activity / plasma membrane-derived thylakoid membrane / photosynthesis, light reaction / ubiquinone binding / quinone binding / electron transport coupled proton transport ...: / Translocases; Catalysing the translocation of protons; Linked to oxidoreductase reactions / photosynthetic electron transport chain / oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor / NADH dehydrogenase activity / plasma membrane-derived thylakoid membrane / photosynthesis, light reaction / ubiquinone binding / quinone binding / electron transport coupled proton transport / ATP synthesis coupled electron transport / NADH dehydrogenase (ubiquinone) activity / aerobic respiration / NAD binding / 4 iron, 4 sulfur cluster binding / iron ion binding / plasma membrane Similarity search - Function | ||||||||||||
Biological species | Thermosynechococcus elongatus BP-1 (bacteria) | ||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.1 Å | ||||||||||||
Authors | Laughlin, T.G. / Bayne, A. / Trempe, J.-F. / Savage, D.F. / Davies, K.M. | ||||||||||||
Funding support | United States, 3items
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Citation | Journal: Nature / Year: 2019 Title: Structure of the complex I-like molecule NDH of oxygenic photosynthesis. Authors: Thomas G Laughlin / Andrew N Bayne / Jean-François Trempe / David F Savage / Karen M Davies / Abstract: Cyclic electron flow around photosystem I (PSI) is a mechanism by which photosynthetic organisms balance the levels of ATP and NADPH necessary for efficient photosynthesis. NAD(P)H dehydrogenase-like ...Cyclic electron flow around photosystem I (PSI) is a mechanism by which photosynthetic organisms balance the levels of ATP and NADPH necessary for efficient photosynthesis. NAD(P)H dehydrogenase-like complex (NDH) is a key component of this pathway in most oxygenic photosynthetic organisms and is the last large photosynthetic membrane-protein complex for which the structure remains unknown. Related to the respiratory NADH dehydrogenase complex (complex I), NDH transfers electrons originating from PSI to the plastoquinone pool while pumping protons across the thylakoid membrane, thereby increasing the amount of ATP produced per NADP molecule reduced. NDH possesses 11 of the 14 core complex I subunits, as well as several oxygenic-photosynthesis-specific (OPS) subunits that are conserved from cyanobacteria to plants. However, the three core complex I subunits that are involved in accepting electrons from NAD(P)H are notably absent in NDH, and it is therefore not clear how NDH acquires and transfers electrons to plastoquinone. It is proposed that the OPS subunits-specifically NdhS-enable NDH to accept electrons from its electron donor, ferredoxin. Here we report a 3.1 Å structure of the 0.42-MDa NDH complex from the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1, obtained by single-particle cryo-electron microscopy. Our maps reveal the structure and arrangement of the principal OPS subunits in the NDH complex, as well as an unexpected cofactor close to the plastoquinone-binding site in the peripheral arm. The location of the OPS subunits supports a role in electron transfer and defines two potential ferredoxin-binding sites at the apex of the peripheral arm. These results suggest that NDH could possess several electron transfer routes, which would serve to maximize plastoquinone reduction and avoid deleterious off-target chemistry of the semi-plastoquinone radical. | ||||||||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | Molecule: MolmilJmol/JSmol |
-Downloads & links
-Download
PDBx/mmCIF format | 6nby.cif.gz | 658.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6nby.ent.gz | 539.9 KB | Display | PDB format |
PDBx/mmJSON format | 6nby.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 6nby_validation.pdf.gz | 1.3 MB | Display | wwPDB validaton report |
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Full document | 6nby_full_validation.pdf.gz | 1.4 MB | Display | |
Data in XML | 6nby_validation.xml.gz | 109.2 KB | Display | |
Data in CIF | 6nby_validation.cif.gz | 167.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/nb/6nby ftp://data.pdbj.org/pub/pdb/validation_reports/nb/6nby | HTTPS FTP |
-Related structure data
Related structure data | 0415MC 0416C 0417C 0418C 0419C 0420C 0425C 6nbqC 6nbxC C: citing same article (ref.) M: map data used to model this data |
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Similar structure data | |
EM raw data | EMPIAR-10257 (Title: Structure of NDH the complex I-like molecule of photosynthesis Data size: 1.8 TB Data #1: Unaligned multiframe micrographs for NDH dataset1 [micrographs - multiframe] Data #2: Unaligned multiframe micrographs for NDH dataset2 [micrographs - multiframe]) |
-Links
-Assembly
Deposited unit |
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1 |
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-Components
-NAD(P)H-quinone oxidoreductase subunit ... , 12 types, 12 molecules ABCEHIJKLMNO
#1: Protein | Mass: 40565.984 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Thermosynechococcus elongatus BP-1 (bacteria) Strain: BP-1 References: UniProt: Q8DL32, Translocases; Catalysing the translocation of protons; Linked to oxidoreductase reactions |
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#2: Protein | Mass: 55168.543 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Thermosynechococcus elongatus BP-1 (bacteria) Strain: BP-1 References: UniProt: Q8DMR6, Translocases; Catalysing the translocation of protons; Linked to oxidoreductase reactions |
#3: Protein | Mass: 15013.919 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Thermosynechococcus elongatus BP-1 (bacteria) Strain: BP-1 References: UniProt: Q8DJ02, Translocases; Catalysing the translocation of protons; Linked to oxidoreductase reactions |
#5: Protein | Mass: 11140.265 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Thermosynechococcus elongatus BP-1 (bacteria) Strain: BP-1 References: UniProt: Q8DL29, Oxidoreductases; Acting on NADH or NADPH; With a quinone or similar compound as acceptor |
#8: Protein | Mass: 45271.184 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Thermosynechococcus elongatus BP-1 (bacteria) Strain: BP-1 References: UniProt: Q8DJD9, Oxidoreductases; Acting on NADH or NADPH; With a quinone or similar compound as acceptor |
#9: Protein | Mass: 22444.801 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Thermosynechococcus elongatus BP-1 (bacteria) Strain: BP-1 References: UniProt: Q8DL31, Oxidoreductases; Acting on NADH or NADPH; With a quinone or similar compound as acceptor |
#10: Protein | Mass: 19363.789 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Thermosynechococcus elongatus BP-1 (bacteria) Strain: BP-1 References: UniProt: Q8DJ01, Oxidoreductases; Acting on NADH or NADPH; With a quinone or similar compound as acceptor |
#11: Protein | Mass: 25766.998 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Thermosynechococcus elongatus BP-1 (bacteria) Strain: BP-1 References: UniProt: Q8DKZ4, Oxidoreductases; Acting on NADH or NADPH; With a quinone or similar compound as acceptor |
#12: Protein | Mass: 8575.137 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Thermosynechococcus elongatus BP-1 (bacteria) Strain: BP-1 References: UniProt: Q8DKZ3, Oxidoreductases; Acting on NADH or NADPH; With a quinone or similar compound as acceptor |
#13: Protein | Mass: 12584.056 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Thermosynechococcus elongatus BP-1 (bacteria) Strain: BP-1 References: UniProt: Q8DLN5, Oxidoreductases; Acting on NADH or NADPH; With a quinone or similar compound as acceptor |
#14: Protein | Mass: 16656.182 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Thermosynechococcus elongatus BP-1 (bacteria) Strain: BP-1 References: UniProt: Q8DJU2, Oxidoreductases; Acting on NADH or NADPH; With a quinone or similar compound as acceptor |
#15: Protein | Mass: 7877.076 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Thermosynechococcus elongatus BP-1 (bacteria) Strain: BP-1 References: UniProt: Q8DMU4, Oxidoreductases; Acting on NADH or NADPH; With a quinone or similar compound as acceptor |
-Protein , 4 types, 4 molecules DFGS
#4: Protein | Mass: 57847.504 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Thermosynechococcus elongatus BP-1 (bacteria) Strain: BP-1 References: UniProt: Q8DKY0, Oxidoreductases; Acting on NADH or NADPH; With a quinone or similar compound as acceptor |
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#6: Protein | Mass: 72025.352 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Thermosynechococcus elongatus BP-1 (bacteria) Strain: BP-1 / References: UniProt: Q8DKX9 |
#7: Protein | Mass: 21580.568 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Thermosynechococcus elongatus BP-1 (bacteria) Strain: BP-1 / References: UniProt: Q8DL30, NADH dehydrogenase (quinone) |
#18: Protein | Mass: 12462.559 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Thermosynechococcus elongatus BP-1 (bacteria) Strain: BP-1 / References: UniProt: Q8DL61 |
-Proton-translocating NADH-quinone dehydrogenase subunit ... , 2 types, 2 molecules PQ
#16: Protein/peptide | Mass: 4878.649 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Thermosynechococcus elongatus BP-1 (bacteria) Strain: BP-1 |
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#17: Protein/peptide | Mass: 4844.698 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Thermosynechococcus elongatus BP-1 (bacteria) Strain: BP-1 |
-Non-polymers , 1 types, 3 molecules
#19: Chemical |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
-Sample preparation
Component | Name: NAD(P)H dehydrogenase-like complex (NDH/NDH-1_1/NDH1L) from T.elongatus Type: COMPLEX / Details: composite model / Entity ID: #1-#8, #10-#18 / Source: NATURAL | ||||||||||||||||
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Molecular weight | Value: 0.42 MDa / Experimental value: YES | ||||||||||||||||
Source (natural) | Organism: Thermosynechococcus elongatus BP-1 (bacteria) | ||||||||||||||||
Buffer solution | pH: 6 | ||||||||||||||||
Buffer component |
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Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||
Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 295 K |
-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: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
Electron lens | Mode: BRIGHT FIELD |
Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
-Processing
EM software |
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||
Symmetry | Point symmetry: C1 (asymmetric) | ||||||||||||||||
3D reconstruction | Resolution: 3.1 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 81670 / Algorithm: BACK PROJECTION Details: A bulk of the model is comprise of EMD-0415 which is at an estimated resolution of 3.1 A, while a portion (NdhF/NdhF1, NdhQ, and NdhC) are from EMD-0425 which is at an estimated resolution of 3.5 A. Symmetry type: POINT | ||||||||||||||||
Atomic model building | B value: 30 / Protocol: RIGID BODY FIT / Space: REAL / Target criteria: Correlation coefficient | ||||||||||||||||
Atomic model building |
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Refinement | Highest resolution: 3.1 Å |