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Yorodumi- PDB-8esz: Structure of mitochondrial complex I from Drosophila melanogaster... -
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-Basic information
Entry | Database: PDB / ID: 8esz | ||||||
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Title | Structure of mitochondrial complex I from Drosophila melanogaster, Helix-locked state | ||||||
Components |
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Keywords | OXIDOREDUCTASE / NADH:ubiquinone oxidoreductase / TRANSLOCASE | ||||||
Function / homology | Function and homology information Mitochondrial protein import / Respiratory electron transport / Complex I biogenesis / Mitochondrial Fatty Acid Beta-Oxidation / RHOG GTPase cycle / Protein lipoylation / Mitochondrial protein degradation / regulation of terminal button organization / Neutrophil degranulation / mitochondrial [2Fe-2S] assembly complex ...Mitochondrial protein import / Respiratory electron transport / Complex I biogenesis / Mitochondrial Fatty Acid Beta-Oxidation / RHOG GTPase cycle / Protein lipoylation / Mitochondrial protein degradation / regulation of terminal button organization / Neutrophil degranulation / mitochondrial [2Fe-2S] assembly complex / ubiquinone-6 biosynthetic process / cellular respiration / NADH:ubiquinone reductase (H+-translocating) / mitochondrial ATP synthesis coupled electron transport / respiratory chain complex I / : / mitochondrial respiratory chain complex I assembly / mitochondrial electron transport, NADH to ubiquinone / electron transport coupled proton transport / acyl binding / acyl carrier activity / NADH dehydrogenase (ubiquinone) activity / ATP synthesis coupled electron transport / quinone binding / : / aerobic respiration / respiratory electron transport chain / proton transmembrane transport / reactive oxygen species metabolic process / determination of adult lifespan / response to reactive oxygen species / mitochondrial membrane / mitochondrial intermembrane space / 2 iron, 2 sulfur cluster binding / NAD binding / FMN binding / 4 iron, 4 sulfur cluster binding / response to oxidative stress / mitochondrial inner membrane / oxidoreductase activity / mitochondrial matrix / protein-containing complex binding / mitochondrion / metal ion binding / cytoplasm Similarity search - Function | ||||||
Biological species | Drosophila melanogaster (fruit fly) | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.4 Å | ||||||
Authors | Padavannil, A. / Letts, J.A. | ||||||
Funding support | United States, 1items
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Citation | Journal: Elife / Year: 2023 Title: Resting mitochondrial complex I from adopts a helix-locked state. Authors: Abhilash Padavannil / Anjaneyulu Murari / Shauna-Kay Rhooms / Edward Owusu-Ansah / James A Letts / Abstract: Respiratory complex I is a proton-pumping oxidoreductase key to bioenergetic metabolism. Biochemical studies have found a divide in the behavior of complex I in metazoans that aligns with the ...Respiratory complex I is a proton-pumping oxidoreductase key to bioenergetic metabolism. Biochemical studies have found a divide in the behavior of complex I in metazoans that aligns with the evolutionary split between Protostomia and Deuterostomia. Complex I from Deuterostomia including mammals can adopt a biochemically defined off-pathway 'deactive' state, whereas complex I from Protostomia cannot. The presence of off-pathway states complicates the interpretation of structural results and has led to considerable mechanistic debate. Here, we report the structure of mitochondrial complex I from the thoracic muscles of the model protostome . We show that although complex I (-CI) does not have a NEM-sensitive deactive state, it does show slow activation kinetics indicative of an off-pathway resting state. The resting-state structure of -CI from the thoracic muscle reveals multiple conformations. We identify a helix-locked state in which an N-terminal α-helix on the NDUFS4 subunit wedges between the peripheral and membrane arms. Comparison of the -CI structure and conformational states to those observed in bacteria, yeast, and mammals provides insight into the roles of subunits across organisms, explains why the -CI off-pathway resting state is NEM insensitive, and raises questions regarding current mechanistic models of complex I turnover. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 8esz.cif.gz | 1.5 MB | Display | PDBx/mmCIF format |
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PDB format | pdb8esz.ent.gz | Display | PDB format | |
PDBx/mmJSON format | 8esz.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 8esz_validation.pdf.gz | 3.6 MB | Display | wwPDB validaton report |
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Full document | 8esz_full_validation.pdf.gz | 3.7 MB | Display | |
Data in XML | 8esz_validation.xml.gz | 233.4 KB | Display | |
Data in CIF | 8esz_validation.cif.gz | 344.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/es/8esz ftp://data.pdbj.org/pub/pdb/validation_reports/es/8esz | HTTPS FTP |
-Related structure data
Related structure data | 28582MC 8eswC M: map data used to model this data C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-Assembly
Deposited unit |
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1 |
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-Components
+NADH dehydrogenase ... , 29 types, 29 molecules ANS6S3V2S8A8A1AOS5AMBLB6B4B7B5B9BMB8B3C2B1S4A9V3V1A7A5ALA6
-Protein , 6 types, 7 molecules S1S7ACABB2S2A3
#3: Protein | Mass: 78724.250 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Drosophila melanogaster (fruit fly) References: UniProt: Q94511, NADH:ubiquinone reductase (H+-translocating) | ||||||
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#6: Protein | Mass: 24622.855 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Drosophila melanogaster (fruit fly) / References: UniProt: Q9VXK7 | ||||||
#25: Protein | Mass: 17257.992 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Drosophila melanogaster (fruit fly) / References: UniProt: Q94519 #30: Protein | | Mass: 10758.288 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Drosophila melanogaster (fruit fly) / References: UniProt: Q7PL91 #31: Protein | | Mass: 52985.953 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Drosophila melanogaster (fruit fly) / References: UniProt: Q9V4E0 #36: Protein | | Mass: 8412.455 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Drosophila melanogaster (fruit fly) / References: UniProt: Q9W380 |
-NADH-ubiquinone oxidoreductase chain ... , 7 types, 7 molecules 14524L63
#8: Protein | Mass: 36383.520 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Drosophila melanogaster (fruit fly) References: UniProt: C7DZL9, NADH:ubiquinone reductase (H+-translocating) |
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#9: Protein | Mass: 51383.047 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Drosophila melanogaster (fruit fly) References: UniProt: Q9MDK5, NADH:ubiquinone reductase (H+-translocating) |
#10: Protein | Mass: 65777.867 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Drosophila melanogaster (fruit fly) References: UniProt: C7DZL4, NADH:ubiquinone reductase (H+-translocating) |
#34: Protein | Mass: 39839.887 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Drosophila melanogaster (fruit fly) References: UniProt: P03896, NADH:ubiquinone reductase (H+-translocating) |
#37: Protein | Mass: 11363.853 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Drosophila melanogaster (fruit fly) References: UniProt: P18934, NADH:ubiquinone reductase (H+-translocating) |
#38: Protein | Mass: 20083.594 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Drosophila melanogaster (fruit fly) References: UniProt: P18933, NADH:ubiquinone reductase (H+-translocating) |
#39: Protein | Mass: 13572.529 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Drosophila melanogaster (fruit fly) References: UniProt: P18930, NADH:ubiquinone reductase (H+-translocating) |
-Non-polymers , 15 types, 68 molecules
#43: Chemical | ChemComp-CDL / #44: Chemical | ChemComp-PC1 / #45: Chemical | ChemComp-ZN / | #46: Chemical | ChemComp-SF4 / #47: Chemical | #48: Chemical | ChemComp-3PE / #49: Chemical | ChemComp-U10 / | #50: Chemical | #51: Chemical | #52: Chemical | ChemComp-OCT / | #53: Chemical | ChemComp-D12 / #54: Chemical | ChemComp-NDP / | #55: Chemical | ChemComp-FMN / | #56: Chemical | ChemComp-WSF / ( | #57: Chemical | ChemComp-DGT / | |
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-Details
Has ligand of interest | N |
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Has protein modification | Y |
-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: Mitochondrial complex I from the thoracic muscle of Drosophila melanogaster Type: COMPLEX / Entity ID: #1-#24, #26-#42, #25 / Source: NATURAL |
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Molecular weight | Experimental value: NO |
Source (natural) | Organism: Drosophila melanogaster (fruit fly) |
Buffer solution | pH: 7.7 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Cryogen name: ETHANE |
-Electron microscopy imaging
Microscopy | Model: TFS GLACIOS |
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Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 200 kV / Illumination mode: FLOOD BEAM |
Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 3000 nm / Nominal defocus min: 500 nm |
Image recording | Electron dose: 60 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
-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: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 293389 / Symmetry type: POINT | ||||||||||||||||||||||||
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