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- EMDB-11873: Cryo-EM structure of Arabidopsis thaliana Complex-I (peripheral arm) -

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Basic information

Entry
Database: EMDB / ID: EMD-11873
TitleCryo-EM structure of Arabidopsis thaliana Complex-I (peripheral arm)
Map data
Sample
  • Complex: Arabidopsis complex I - peripheral arm
    • Protein or peptide: x 17 types
  • Ligand: x 6 types
Function / homology
Function and homology information


cold acclimation / photorespiration / embryo development ending in seed dormancy / respiratory chain complex I / cobalt ion binding / response to osmotic stress / plastid / acyl carrier activity / NADH:ubiquinone reductase (H+-translocating) / mitochondrial respiratory chain complex I ...cold acclimation / photorespiration / embryo development ending in seed dormancy / respiratory chain complex I / cobalt ion binding / response to osmotic stress / plastid / acyl carrier activity / NADH:ubiquinone reductase (H+-translocating) / mitochondrial respiratory chain complex I / mitochondrial respiratory chain complex I assembly / mitochondrial electron transport, NADH to ubiquinone / NADH dehydrogenase (ubiquinone) activity / quinone binding / ATP synthesis coupled electron transport / respiratory electron transport chain / chloroplast / mitochondrial membrane / 2 iron, 2 sulfur cluster binding / NAD binding / FMN binding / 4 iron, 4 sulfur cluster binding / mitochondrial matrix / mitochondrion / zinc ion binding / extracellular region / metal ion binding / nucleus / plasma membrane / cytosol
Similarity search - Function
NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial / Soluble ligand binding domain / SLBB domain / Zinc finger, CHCC-type / Zinc-finger domain / GRIM-19 / GRIM-19 protein / NDUFA6, LYR domain / NADH dehydrogenase ubiquinone Fe-S protein 4-like superfamily / NADH dehydrogenase ubiquinone Fe-S protein 4 ...NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial / Soluble ligand binding domain / SLBB domain / Zinc finger, CHCC-type / Zinc-finger domain / GRIM-19 / GRIM-19 protein / NDUFA6, LYR domain / NADH dehydrogenase ubiquinone Fe-S protein 4-like superfamily / NADH dehydrogenase ubiquinone Fe-S protein 4 / NADH dehydrogenase ubiquinone Fe-S protein 4, mitochondrial / NADH dehydrogenase [ubiquinone] (complex I), alpha subcomplex, subunit 2 / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12 / NADH ubiquinone oxidoreductase subunit NDUFA12 / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5 / ETC complex I subunit conserved region / NADH dehydrogenase [ubiquinone] (complex I), alpha subcomplex, subunit 6 / NADH-quinone oxidoreductase, chain G, C-terminal / NADH-ubiquinone oxidoreductase subunit G, C-terminal / Respiratory-chain NADH dehydrogenase 20 Kd subunit signature. / NADH-ubiquinone oxidoreductase, 20 Kd subunit / NADH-quinone oxidoreductase, chain I / NAD(P)H-quinone oxidoreductase subunit D/H / NADH:ubiquinone oxidoreductase, 49kDa subunit, conserved site / Respiratory chain NADH dehydrogenase 49 Kd subunit signature. / NADH-quinone oxidoreductase, subunit D / Respiratory-chain NADH dehydrogenase, 49 Kd subunit / NADH:ubiquinone oxidoreductase, subunit G / Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 3. / Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 2. / NADH dehydrogenase, subunit C / NADH ubiquinone oxidoreductase, F subunit / NADH:ubiquinone oxidoreductase, 30kDa subunit, conserved site / Respiratory chain NADH dehydrogenase 30 Kd subunit signature. / 2Fe-2S iron-sulfur cluster binding domain / Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 1. / NADH:ubiquinone oxidoreductase, 75kDa subunit, conserved site / NADH:ubiquinone oxidoreductase, 30kDa subunit / NADH:ubiquinone oxidoreductase, 30kDa subunit superfamily / Respiratory-chain NADH dehydrogenase, 30 Kd subunit / NADH-ubiquinone oxidoreductase-G iron-sulfur binding region / NADH-ubiquinone oxidoreductase-G iron-sulfur binding region / Respiratory-chain NADH dehydrogenase 51 Kd subunit signature 1. / Respiratory-chain NADH dehydrogenase 24 Kd subunit signature. / NuoE domain / NADH-quinone oxidoreductase subunit E-like / Thioredoxin-like [2Fe-2S] ferredoxin / NADH-quinone oxidoreductase subunit E, N-terminal / NADH:ubiquinone oxidoreductase, subunit G, iron-sulphur binding / His(Cys)3-ligated-type [4Fe-4S] domain profile. / NADH:ubiquinone oxidoreductase, 51kDa subunit, conserved site / Respiratory-chain NADH dehydrogenase 51 Kd subunit signature 2. / NADH-ubiquinone oxidoreductase 51kDa subunit, FMN-binding domain / NADH-ubiquinone oxidoreductase 51kDa subunit, iron-sulphur binding domain / NADH-ubiquinone oxidoreductase 51kDa subunit, iron-sulphur binding domain superfamily / NADH-ubiquinone oxidoreductase 51kDa subunit, FMN-binding domain superfamily / Respiratory-chain NADH dehydrogenase 51 Kd subunit / NADH-ubiquinone oxidoreductase-F iron-sulfur binding region / NADH-ubiquinone oxidoreductase-F iron-sulfur binding region / Molybdopterin oxidoreductase, 4Fe-4S domain / Prokaryotic molybdopterin oxidoreductases 4Fe-4S domain profile. / NAD-dependent epimerase/dehydratase / NAD dependent epimerase/dehydratase family / NADH:ubiquinone oxidoreductase-like, 20kDa subunit / NADH ubiquinone oxidoreductase, 20 Kd subunit / Molybdopterin oxidoreductase / Molybdopterin oxidoreductase / [NiFe]-hydrogenase, large subunit / Ribosomal protein/NADH dehydrogenase domain / Mitochondrial ribosomal protein L51 / S25 / CI-B8 domain / Mitochondrial ribosomal protein L51 / S25 / CI-B8 domain / Acyl carrier protein (ACP) / 4Fe-4S dicluster domain / 2Fe-2S ferredoxin-type iron-sulfur binding domain profile. / 2Fe-2S ferredoxin-type iron-sulfur binding domain / 2Fe-2S ferredoxin-like superfamily / Phosphopantetheine attachment site / Phosphopantetheine attachment site. / 4Fe-4S ferredoxin, iron-sulphur binding, conserved site / 4Fe-4S ferredoxin-type iron-sulfur binding region signature. / 4Fe-4S ferredoxin-type iron-sulfur binding domain profile. / 4Fe-4S ferredoxin-type, iron-sulphur binding domain / Phosphopantetheine attachment site / ACP-like superfamily / Carrier protein (CP) domain profile. / Phosphopantetheine binding ACP domain / Thioredoxin-like superfamily / NAD(P)-binding domain superfamily
Similarity search - Domain/homology
NADH dehydrogenase [ubiquinone] iron-sulfur protein 2 / NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial / Acyl carrier protein 2, mitochondrial / NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial / NADH dehydrogenase [ubiquinone] iron-sulfur protein 8-A, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13-A / NADH dehydrogenase [ubiquinone] iron-sulfur protein 3 / NADH dehydrogenase [ubiquinone] iron-sulfur protein 1, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2 / NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial ...NADH dehydrogenase [ubiquinone] iron-sulfur protein 2 / NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial / Acyl carrier protein 2, mitochondrial / NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial / NADH dehydrogenase [ubiquinone] iron-sulfur protein 8-A, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13-A / NADH dehydrogenase [ubiquinone] iron-sulfur protein 3 / NADH dehydrogenase [ubiquinone] iron-sulfur protein 1, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2 / NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial / Probable NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5, mitochondrial / NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6 / NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial / Probable NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12 / Furry / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial
Similarity search - Component
Biological speciesArabidopsis thaliana (thale cress) / Mouse-ear cress (thale cress)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.91 Å
AuthorsKlusch N / Kuehlbrandt W / Yildiz O
Funding support Germany, 1 items
OrganizationGrant numberCountry
Max Planck Society Germany
CitationJournal: Plant Cell / Year: 2021
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
DepositionOct 22, 2020-
Header (metadata) releaseDec 8, 2021-
Map releaseDec 8, 2021-
UpdateDec 8, 2021-
Current statusDec 8, 2021Processing site: PDBe / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.011
  • Imaged by UCSF Chimera
  • Download
  • Surface view colored by height
  • Surface level: 0.011
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-7aqr
  • Surface level: 0.011
  • Imaged by UCSF Chimera
  • Download
Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_11873.png

Downloads & links

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Map

FileDownload / File: emd_11873.map.gz / Format: CCP4 / Size: 824 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Voxel sizeX=Y=Z: 0.837 Å
Density
Contour LevelBy AUTHOR: 0.011 / Movie #1: 0.011
Minimum - Maximum-0.035325088 - 0.08330584
Average (Standard dev.)2.7374539e-05 (±0.0007684718)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions600600600
Spacing600600600
CellA=B=C: 502.2 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z0.8370.8370.837
M x/y/z600600600
origin x/y/z0.0000.0000.000
length x/y/z502.200502.200502.200
α/β/γ90.00090.00090.000
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS600600600
D min/max/mean-0.0350.0830.000

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Supplemental data

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Half map: #2

Fileemd_11873_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #1

Fileemd_11873_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Arabidopsis complex I - peripheral arm

EntireName: Arabidopsis complex I - peripheral arm
Components
  • Complex: Arabidopsis complex I - peripheral arm
    • Protein or peptide: NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] iron-sulfur protein 3
    • Protein or peptide: NADH dehydrogenase subunit 7
    • Protein or peptide: NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] iron-sulfur protein 1, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] iron-sulfur protein 8-A, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2
    • Protein or peptide: Acyl carrier protein 2, mitochondrial
    • Protein or peptide: Probable NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13-A
    • Protein or peptide: Probable NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12
    • Protein or peptide: Furry
  • Ligand: IRON/SULFUR CLUSTERIron–sulfur cluster
  • Ligand: FE2/S2 (INORGANIC) CLUSTER
  • Ligand: FLAVIN MONONUCLEOTIDE
  • Ligand: NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
  • Ligand: ZINC ION
  • Ligand: S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl] dodecanethioate

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Supramolecule #1: Arabidopsis complex I - peripheral arm

SupramoleculeName: Arabidopsis complex I - peripheral arm / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#17
Source (natural)Organism: Arabidopsis thaliana (thale cress)

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Macromolecule #1: NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial
type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Mouse-ear cress (thale cress)
Molecular weightTheoretical: 24.071949 KDa
SequenceString: MAMITRNTAT RLPLLLQSQR AVAAASVSHL HTSLPALSPS TSPTSYTRPG PPSTSPPPPG LSKAAEFVIS KVDDLMNWAR TGSIWPMTF GLACCAVEMM HTGAARYDLD RFGIIFRPSP RQSDCMIVAG TLTNKMAPAL RKVYDQMPEP RWVISMGSCA N GGGYYHYS ...String:
MAMITRNTAT RLPLLLQSQR AVAAASVSHL HTSLPALSPS TSPTSYTRPG PPSTSPPPPG LSKAAEFVIS KVDDLMNWAR TGSIWPMTF GLACCAVEMM HTGAARYDLD RFGIIFRPSP RQSDCMIVAG TLTNKMAPAL RKVYDQMPEP RWVISMGSCA N GGGYYHYS YSVVRGCDRI VPVDIYVPGC PPTAEALLYG LLQLQKKINR RKDFLHWWNK

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Macromolecule #2: NADH dehydrogenase [ubiquinone] iron-sulfur protein 3

MacromoleculeName: NADH dehydrogenase [ubiquinone] iron-sulfur protein 3 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Mouse-ear cress (thale cress)
Molecular weightTheoretical: 22.91091 KDa
SequenceString:
MDNQFIFKYS WETLPKKWVK KMERSEHGNR FDTNTDYLFQ LLCFLKLHTY TRVQVLIDIC GVDYPSRKRR FEVVYNLLST RYNSRIRVQ TSADEVTRIS SVVSLFPSAG WWEREVWDMF GVSFINHPDL RRILTDYGFE GHPLRKDFPL SGYVQVRYDD P EKRVVSEP IEMTQEFRYF DFASPWEQRS DG

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Macromolecule #3: NADH dehydrogenase subunit 7

MacromoleculeName: NADH dehydrogenase subunit 7 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mouse-ear cress (thale cress)
Molecular weightTheoretical: 45.036844 KDa
SequenceString: MTTRKRQIKN FTLNFGPQHP AAHGVLRLVL EMNGEVVERA EPHIGLLHRG TEKLIEYKTY LQALPYFDRL DYVSMMAQEH AYSLAVEKL LNCEVPLRAQ YIRVLFCEIT RILNHLLALT THAMDVGALT PFLWAFEERE KLLEFYERVS GARMHASFIR P GGVAQDLP ...String:
MTTRKRQIKN FTLNFGPQHP AAHGVLRLVL EMNGEVVERA EPHIGLLHRG TEKLIEYKTY LQALPYFDRL DYVSMMAQEH AYSLAVEKL LNCEVPLRAQ YIRVLFCEIT RILNHLLALT THAMDVGALT PFLWAFEERE KLLEFYERVS GARMHASFIR P GGVAQDLP LGLCRDIDSF TQQFASRIDE LEEMLTGNRI WKQRLVDIGT VTAQQAKDWG FSGVMLRGSG VCWDLRRAAP YD VYDQLDF DVPVGTRGDC YDRYCIRIEE MRQSLRIIVQ CLNQMPSGMI KADDRKLCPP SRCRMKLSME SLIHHFELYT EGF SVPASS TYTAVEAPKG EFGVFLVSNG SNRPYRCKIR APGFAHSQGL DFMSKHHMLA DVVTIIGTQD IVFGEVDR

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Macromolecule #4: NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial
type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Mouse-ear cress (thale cress)
Molecular weightTheoretical: 28.423607 KDa
SequenceString: MLARLAAKRL LEIRQVFRQP TSQVTRSLST ALNYHLDSPD NKPDLPWEFS EANQSKVKEI LSYYPSNYKQ SAVIPLLDLA QQQNGGWLP VSAMNAVAKV IEVAPIRVYE VATFYSMFNR AKVGKYHLLV CGTTPCMIRG SRDIESALLD HLGVKRGEVT K DGLFSVGE ...String:
MLARLAAKRL LEIRQVFRQP TSQVTRSLST ALNYHLDSPD NKPDLPWEFS EANQSKVKEI LSYYPSNYKQ SAVIPLLDLA QQQNGGWLP VSAMNAVAKV IEVAPIRVYE VATFYSMFNR AKVGKYHLLV CGTTPCMIRG SRDIESALLD HLGVKRGEVT K DGLFSVGE MECMGCCVNA PMITVADYSN GSEGYTYNYF EDVTPEKVVE IVEKLRKGEK PPHGTQNPKR IKCGPEGGNK TL LGEPKPP QFRDLDAC

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Macromolecule #5: NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial
type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Mouse-ear cress (thale cress)
Molecular weightTheoretical: 53.522418 KDa
SequenceString: MAPVRGILGL QRAVSIWKES NRLTPALRSF STQAASTSTT PQPPPPPPPP EKTHFGGLKD EDRIFTNLYG LHDPFLKGAM KRGDWHRTK DLVLKGTDWI VNEMKKSGLR GRGGAGFPSG LKWSFMPKVS DGRPSYLVVN ADESEPGTCK DREIMRHDPH K LLEGCLIA ...String:
MAPVRGILGL QRAVSIWKES NRLTPALRSF STQAASTSTT PQPPPPPPPP EKTHFGGLKD EDRIFTNLYG LHDPFLKGAM KRGDWHRTK DLVLKGTDWI VNEMKKSGLR GRGGAGFPSG LKWSFMPKVS DGRPSYLVVN ADESEPGTCK DREIMRHDPH K LLEGCLIA GVGMRASAAY IYIRGEYVNE RLNLEKARRE AYAAGLLGKN ACGSGYDFEV YIHFGAGAYI CGEETALLES LE GKQGKPR LKPPFPANAG LYGCPTTVTN VETVAVSPTI LRRGPEWFSS FGRKNNAGTK LFCISGHVNK PCTVEEEMSI PLK ELIERH CGGVRGGWDN LLAIIPGGSS VPLIPKNICE DVLMDFDALK AVQSGLGTAA VIVMDKSTDV VDAIARLSYF YKHE SCGQC TPCREGTGWL WMIMERMKVG NAKLEEIDML QEVTKQIEGH TICALGDAAA WPVQGLIRHF RPELERRIRE RAERE LLQA AA

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Macromolecule #6: NADH dehydrogenase [ubiquinone] iron-sulfur protein 1, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] iron-sulfur protein 1, mitochondrial
type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Mouse-ear cress (thale cress)
Molecular weightTheoretical: 81.619367 KDa
SequenceString: MGLGILASRT IRPASRLLQS QTSNFFLRTI VSKPELQSPE SAAVSEPEPP TQILPPRNPV GGARVHFSNP EDAIEVFVDG YAVKVPKGF TVLQACEVAG VDIPRFCYHS RLSIAGNCRM CLVEVEKSPK PVASCAMPAL PGMKIKTDTP IAKKAREGVM E FLLMNHPL ...String:
MGLGILASRT IRPASRLLQS QTSNFFLRTI VSKPELQSPE SAAVSEPEPP TQILPPRNPV GGARVHFSNP EDAIEVFVDG YAVKVPKGF TVLQACEVAG VDIPRFCYHS RLSIAGNCRM CLVEVEKSPK PVASCAMPAL PGMKIKTDTP IAKKAREGVM E FLLMNHPL DCPICDQGGE CDLQDQSMAF GSDRGRFTEM KRSVVDKNLG PLVKTVMTRC IQCTRCVRFA SEVAGVQDLG IL GRGSGEE IGTYVEKLMT SELSGNVIDI CPVGALTSKP FAFKARNWEL KATETIDVSD AVGSNIRVDS RGPEVMRIIP RLN EDINEE WISDKTRFCY DGLKRQRLSD PMIRDSDGRF KAVSWRDALA VVGDIIHQVK PDEIVGVAGQ LSDAESMMVL KDFV NRMGS DNVWCEGTAA GVDADLRYSY LMNTSISGLE NADLFLLIGT QPRVEAAMVN ARICKTVRAS NAKVGYVGPP AEFNY DCKH LGTGPDTLKE IAEGRHPFCT ALKNAKNPAI IVGAGLFNRT DKNAILSSVE SIAQANNVVR PDWNGLNFLL QYAAQA AAL DLGLIQQSAK ALESAKFVYL MGADDVNVDK IPKDAFVVYQ GHHGDKAVYR ANVILPASAF TEKEGTYENT EGFTQQT VP AVPTVGDARD DWKIVRALSE VSGVKLPYNS IEGVRSRIKS VAPNLVHTDE REPAAFGPSL KPECKEAMST TPFQTVVE N FYMTNSITRA SKIMAQCSAV LLKKPFV

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Macromolecule #7: NADH dehydrogenase [ubiquinone] iron-sulfur protein 8-A, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] iron-sulfur protein 8-A, mitochondrial
type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Mouse-ear cress (thale cress)
Molecular weightTheoretical: 25.536801 KDa
SequenceString: MASILARRSL NTLRARHLVL SGQALQGSHL SRLQSRGISY GSNKDDEEAE QLSKEISKDW NTVFERSINT LFLTEMVRGL SLTLKYFFD PKVTINYPFE KGPLSPRFRG EHALRRYPTG EERCIACKLC EAVCPAQAIT IEAEEREDGS RRTTRYDIDM T KCIYCGFC ...String:
MASILARRSL NTLRARHLVL SGQALQGSHL SRLQSRGISY GSNKDDEEAE QLSKEISKDW NTVFERSINT LFLTEMVRGL SLTLKYFFD PKVTINYPFE KGPLSPRFRG EHALRRYPTG EERCIACKLC EAVCPAQAIT IEAEEREDGS RRTTRYDIDM T KCIYCGFC QEACPVDAIV EGPNFEFATE THEELLYDKE KLLENGDRWE TEIAENLRSE SLYR

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Macromolecule #8: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mit...

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial
type: protein_or_peptide / ID: 8 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mouse-ear cress (thale cress)
Molecular weightTheoretical: 43.988652 KDa
SequenceString: MQVVSRRLVQ RPLVGGASIY SSSSLRSLYG VSNHLNGTDN CRYSSSLATK GVGHLARKGT GGRSSVSGIV ATVFGATGFL GRYLVQQLA KMGSQVLVPF RGSEDSPRHL KLMGDLGQVV PMKFDPRDED SIKAVMAKAN VVINLIGREY ETRNFSFEDA N HHIAEKLA ...String:
MQVVSRRLVQ RPLVGGASIY SSSSLRSLYG VSNHLNGTDN CRYSSSLATK GVGHLARKGT GGRSSVSGIV ATVFGATGFL GRYLVQQLA KMGSQVLVPF RGSEDSPRHL KLMGDLGQVV PMKFDPRDED SIKAVMAKAN VVINLIGREY ETRNFSFEDA N HHIAEKLA LVAKEHGGIM RYIQVSCLGA SVSSPSRMLR AKAAAEEAVL NALPEATIMR PATMIGTEDR ILNPWSMFVK KY GFLPLIG GGTTKFQPVY VVDVAAAIVA ALKDDGSSMG KTYELGGPDV FTTHELAEIM YDMIREWPRY VKLPFPIAKA MAA PRDFMV NKVPFPLPSP QIFNLDQINA LTTDTLVSDN ALKFQDLDLV PHKLKGYPVE FLIQYRKGGP NFGSTVSEKI PTDF YP

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Macromolecule #9: NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial
type: protein_or_peptide / ID: 9 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mouse-ear cress (thale cress)
Molecular weightTheoretical: 17.160445 KDa
SequenceString:
MALCATTQRT IRIAATLRRV ARPFATDAVV ESDYKRGEIG KVSGIPEEHL SRKVIIYSPA RTATQSGSGK LGKWKINFVS TLKWENPLM GWTSTGDPYA NVGDSALAFD SEEAAKSFAE RHGWDYKVKK PNTPLLKVKS YSDNFKWKGN PQPEN

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Macromolecule #10: NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial
type: protein_or_peptide / ID: 10 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mouse-ear cress (thale cress)
Molecular weightTheoretical: 12.251122 KDa
SequenceString:
MASNLLKALI RSQILPSSRR NFSVATTQLG IPTDDLVGNH TAKWMQDRSK KSPMELISEV PPIKVDGRIV ACEGDTNPAL GHPIEFICL DLNEPAICKY CGLRYVQDHH H

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Macromolecule #11: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2
type: protein_or_peptide / ID: 11 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mouse-ear cress (thale cress)
Molecular weightTheoretical: 10.865765 KDa
SequenceString:
MAWRGSISKS MKELRILLCQ SSPASAPTRT FVEKNYKDLK SLNPKLPILI RECSGVQPQM WARYDMGVER CVNLDGLTEP QILKALENL VKSGATKA

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Macromolecule #12: Acyl carrier protein 2, mitochondrial

MacromoleculeName: Acyl carrier protein 2, mitochondrial / type: protein_or_peptide / ID: 12 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mouse-ear cress (thale cress)
Molecular weightTheoretical: 14.183111 KDa
SequenceString:
MAARGAMLRY LRVNVNPTIQ NPRECVLPFS ILLRRFSEEV RGSFLDKSEV TDRVLSVVKN FQKVDPSKVT PKANFQNDLG LDSLDSVEV VMALEEEFGF EIPDNEADKI QSIDLAVDFI ASHPQAK

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Macromolecule #13: Probable NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subun...

MacromoleculeName: Probable NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5, mitochondrial
type: protein_or_peptide / ID: 13 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mouse-ear cress (thale cress)
Molecular weightTheoretical: 19.201906 KDa
SequenceString:
MFLRAIGRPL LAKVKQTTGI VGLDVVPNAR AVLIDLYSKT LKEIQAVPED EGYRKAVESF TRQRLNVCKE EEDWEMIEKR LGCGQVEEL IEEARDELTL IGKMIEWDPW GVPDDYECEV IENDAPIPKH VPQHRPGPLP EQFYKTLEGL IAESKTEIPA A TPSDPQLK E

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Macromolecule #14: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6
type: protein_or_peptide / ID: 14 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mouse-ear cress (thale cress)
Molecular weightTheoretical: 15.102261 KDa
SequenceString:
MAAPFALRKI GVPPNSANLT EARRRVFDFF RAACRSIPTI MDIYNLQDVV APSQLRYAIS AQIRNNAHIT DPKVIDLLIF KGMEELTDI VDHAKQRHHI IGQYVVGEGL VQNTGNKDQG KTDFLKNFYT SNYF

+
Macromolecule #15: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13-A

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13-A
type: protein_or_peptide / ID: 15 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mouse-ear cress (thale cress)
Molecular weightTheoretical: 16.145584 KDa
SequenceString:
MTEAMIRNKP GMASVKDMPL LQDGPPPGGF APVRYARRIS NTGPSAMAMF LAVSGAFAWG MYQVGQGNKI RRALKEEKYA ARRTILPIL QAEEDERFVS EWKKYLEYEA DVMKDVPGWK VGENVYNSGR WMPPATGELR PDVW

+
Macromolecule #16: Probable NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12

MacromoleculeName: Probable NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12
type: protein_or_peptide / ID: 16 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mouse-ear cress (thale cress)
Molecular weightTheoretical: 18.346736 KDa
SequenceString:
MALTVAKSAL EAIREKGLGG FMRMIREEGF MRCLPDGNLL QTKIHNIGAT LVGVDKFGNK YYQKLGDTQY GRHRWVEYAS KDRYNASQV PAEWHGWLHF ITDHTGDELL SLKPKRYGLE HKENFSGEGD AYIYHSKGHT LNPGQKNWTR YQSWVPTKTQ

+
Macromolecule #17: Furry

MacromoleculeName: Furry / type: protein_or_peptide / ID: 17 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mouse-ear cress (thale cress)
Molecular weightTheoretical: 15.060062 KDa
SequenceString:
MAKSVSTAAS SLVQNLRRYI KKPWQITGPC AHPEYLEAVP KATEYRLRCP ATIDEEAIVP SSDPETVYNI VYHGRDQRRN RPPIRRYVL TKDNVVQMMN EKKSFDVSDF PKVYLTTTVE EDLDTRGGGY EK

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Macromolecule #18: IRON/SULFUR CLUSTER

MacromoleculeName: IRON/SULFUR CLUSTER / type: ligand / ID: 18 / Number of copies: 6 / Formula: SF4
Molecular weightTheoretical: 351.64 Da
Chemical component information

ChemComp-FS1:
IRON/SULFUR CLUSTER / Iron–sulfur cluster

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Macromolecule #19: FE2/S2 (INORGANIC) CLUSTER

MacromoleculeName: FE2/S2 (INORGANIC) CLUSTER / type: ligand / ID: 19 / Number of copies: 2 / Formula: FES
Molecular weightTheoretical: 175.82 Da
Chemical component information

ChemComp-FES:
FE2/S2 (INORGANIC) CLUSTER / Iron–sulfur cluster

+
Macromolecule #20: FLAVIN MONONUCLEOTIDE

MacromoleculeName: FLAVIN MONONUCLEOTIDE / type: ligand / ID: 20 / Number of copies: 1 / Formula: FMN
Molecular weightTheoretical: 456.344 Da
Chemical component information

ChemComp-FMN:
FLAVIN MONONUCLEOTIDE / Flavin mononucleotide

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Macromolecule #21: NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE

MacromoleculeName: NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
type: ligand / ID: 21 / Number of copies: 1 / Formula: NDP
Molecular weightTheoretical: 745.421 Da
Chemical component information

ChemComp-NDP:
NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE / Nicotinamide adenine dinucleotide phosphate

+
Macromolecule #22: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 22 / Number of copies: 1 / Formula: ZN
Molecular weightTheoretical: 65.409 Da

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Macromolecule #23: S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-b...

MacromoleculeName: S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl] dodecanethioate
type: ligand / ID: 23 / Number of copies: 1 / Formula: 8Q1
Molecular weightTheoretical: 540.651 Da
Chemical component information

ChemComp-8Q1:
S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl] dodecanethioate

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.8
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 43.0 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
Final reconstructionResolution.type: BY AUTHOR / Resolution: 2.91 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 3) / Number images used: 459177
FSC plot (resolution estimation)

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