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- EMDB-11241: Peripheral domain of open complex I during turnover -

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Basic information

Entry
Database: EMDB / ID: EMD-11241
TitlePeripheral domain of open complex I during turnover
Map dataOversampled, local resolution-filtered map
Sample
  • Complex: Peripheral domain of open complex I during turnover
    • Protein or peptide: x 18 types
  • Ligand: x 12 types
Function / homology
Function and homology information


NADH dehydrogenase activity / respiratory chain complex I / NADH:ubiquinone reductase (H+-translocating) / mitochondrial respiratory chain complex I / apoptotic mitochondrial changes / mitochondrial respiratory chain complex I assembly / mitochondrial electron transport, NADH to ubiquinone / electron transport chain / NADH dehydrogenase (ubiquinone) activity / ATP synthesis coupled electron transport ...NADH dehydrogenase activity / respiratory chain complex I / NADH:ubiquinone reductase (H+-translocating) / mitochondrial respiratory chain complex I / apoptotic mitochondrial changes / mitochondrial respiratory chain complex I assembly / mitochondrial electron transport, NADH to ubiquinone / electron transport chain / NADH dehydrogenase (ubiquinone) activity / ATP synthesis coupled electron transport / respirasome / ATP metabolic process / reactive oxygen species metabolic process / respiratory electron transport chain / regulation of mitochondrial membrane potential / mitochondrial intermembrane space / 2 iron, 2 sulfur cluster binding / circadian rhythm / fatty acid biosynthetic process / 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 / metal ion binding
Similarity search - Function
Complex1_LYR-like / Soluble ligand binding domain / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7 / NADH:ubiquinone oxidoreductase subunit B14.5a (Complex I-B14.5a) / SLBB domain / 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 ...Complex1_LYR-like / Soluble ligand binding domain / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7 / NADH:ubiquinone oxidoreductase subunit B14.5a (Complex I-B14.5a) / SLBB domain / 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 / 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. / 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 / Molybdopterin oxidoreductase / Molybdopterin oxidoreductase / 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) / 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. / 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] 1 alpha subcomplex subunit 12 / Acyl carrier protein / NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7 / NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial / NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5 / NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2 ...NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12 / Acyl carrier protein / NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7 / NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial / NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5 / NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2 / NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6
Similarity search - Component
Biological speciesOvis aries (sheep) / Sheep (sheep)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.3 Å
AuthorsKampjut D / Sazanov LA
Funding supportEuropean Union, 2 items
OrganizationGrant numberCountry
European Commission665385European Union
European Commission653706European Union
CitationJournal: Science / Year: 2020
Title: The coupling mechanism of mammalian respiratory complex I.
Authors: Domen Kampjut / Leonid A Sazanov /
Abstract: Mitochondrial complex I couples NADH:ubiquinone oxidoreduction to proton pumping by an unknown mechanism. Here, we present cryo-electron microscopy structures of ovine complex I in five different ...Mitochondrial complex I couples NADH:ubiquinone oxidoreduction to proton pumping by an unknown mechanism. Here, we present cryo-electron microscopy structures of ovine complex I in five different conditions, including turnover, at resolutions up to 2.3 to 2.5 angstroms. Resolved water molecules allowed us to experimentally define the proton translocation pathways. Quinone binds at three positions along the quinone cavity, as does the inhibitor rotenone that also binds within subunit ND4. Dramatic conformational changes around the quinone cavity couple the redox reaction to proton translocation during open-to-closed state transitions of the enzyme. In the induced deactive state, the open conformation is arrested by the ND6 subunit. We propose a detailed molecular coupling mechanism of complex I, which is an unexpected combination of conformational changes and electrostatic interactions.
History
DepositionJun 30, 2020-
Header (metadata) releaseOct 7, 2020-
Map releaseOct 7, 2020-
UpdateDec 2, 2020-
Current statusDec 2, 2020Processing site: PDBe / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.105
  • Imaged by UCSF Chimera
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  • Surface view colored by height
  • Surface level: 0.105
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-6zk9
  • Surface level: 0.105
  • Imaged by UCSF Chimera
  • Download
  • Simplified surface model + fitted atomic model
  • Atomic modelsPDB-6zk9
  • Imaged by Jmol
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_11241.png

Downloads & links

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Map

FileDownload / File: emd_11241.map.gz / Format: CCP4 / Size: 134.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationOversampled, local resolution-filtered map
Voxel sizeX=Y=Z: 0.5 Å
Density
Contour LevelBy AUTHOR: 0.105 / Movie #1: 0.105
Minimum - Maximum-0.30611384 - 0.8862452
Average (Standard dev.)0.008886407 (±0.052853063)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions321294374
Spacing294321374
CellA: 147.0 Å / B: 160.5 Å / C: 187.0 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z0.50.50.5
M x/y/z294321374
origin x/y/z0.0000.0000.000
length x/y/z147.000160.500187.000
α/β/γ90.00090.00090.000
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS294321374
D min/max/mean-0.3060.8860.009

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Supplemental data

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Sample components

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Entire : Peripheral domain of open complex I during turnover

EntireName: Peripheral domain of open complex I during turnover
Components
  • Complex: Peripheral domain of open complex I during turnover
    • Protein or peptide: NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial
    • Protein or peptide: Mitochondrial complex I, 24 kDa subunit
    • Protein or peptide: NADH:ubiquinone oxidoreductase core subunit S1
    • Protein or peptide: Mitochondrial complex I, 49 kDa subunit
    • Protein or peptide: NADH:ubiquinone oxidoreductase core subunit S3
    • Protein or peptide: Mitochondrial complex I, PSST subunit
    • Protein or peptide: Mitochondrial complex I, TYKY subunit
    • Protein or peptide: Mitochondrial complex I, 10 kDa subunit
    • Protein or peptide: Mitochondrial complex I, 13 kDa subunit
    • Protein or peptide: NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial
    • Protein or peptide: NADH:ubiquinone oxidoreductase subunit A9
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2
    • Protein or peptide: Mitochondrial complex I, B13 subunit
    • Protein or peptide: NADH:ubiquinone oxidoreductase subunit A6
    • Protein or peptide: Mitochondrial complex I, B14.5a subunit
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12
    • Protein or peptide: Acyl carrier protein
    • Protein or peptide: Mitochondrial complex I, B16.6 subunit
  • Ligand: IRON/SULFUR CLUSTERIron–sulfur cluster
  • Ligand: FLAVIN MONONUCLEOTIDE
  • Ligand: 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE
  • Ligand: FE2/S2 (INORGANIC) CLUSTER
  • Ligand: POTASSIUM IONPotassium
  • Ligand: 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE
  • Ligand: 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOETHANOLAMINE
  • Ligand: ZINC ION
  • Ligand: NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
  • Ligand: S-[2-({N-[(2S)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl] tetradecanethioate
  • Ligand: CARDIOLIPIN
  • Ligand: water

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Supramolecule #1: Peripheral domain of open complex I during turnover

SupramoleculeName: Peripheral domain of open complex I during turnover / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#18
Source (natural)Organism: Ovis aries (sheep)
Molecular weightExperimental: 1 MDa

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

MacromoleculeName: NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial
type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH dehydrogenase
Source (natural)Organism: Sheep (sheep)
Molecular weightTheoretical: 50.68775 KDa
SequenceString: MLAARRLLGG SLPARVSVRF SGDTTAPKKT SFGSLKDEDR IFTNLYGRHD WRLKGAQSRG DWYKTKEILL KGPDWILGEV KTSGLRGRG GAGFPTGLKW SFMNKPSDGR PKYLVVNADE GEPGTCKDRE IIRHDPHKLV EGCLVGGRAM GARAAYIYIR G EFYNEASN ...String:
MLAARRLLGG SLPARVSVRF SGDTTAPKKT SFGSLKDEDR IFTNLYGRHD WRLKGAQSRG DWYKTKEILL KGPDWILGEV KTSGLRGRG GAGFPTGLKW SFMNKPSDGR PKYLVVNADE GEPGTCKDRE IIRHDPHKLV EGCLVGGRAM GARAAYIYIR G EFYNEASN LQVAIREAYE AGLIGKNACG SGYDFDVFVV RGAGAYICGE ETALIESIEG KQGKPRLKPP FPADVGVFGC PT TVANVET VAVSPTICRR GGAWFASFGR ERNSGTKLFN ISGHVNNPCT VEEEMSVPLK ELIEKHAGGV TGGWDNLLAV IPG GSSTPL IPKSVCETVL MDFDALIQAQ TGLGTAAVIV MDRSTDIVKA IARLIEFYKH ESCGQCTPCR EGVDWMNKVM ARFV RGDAR PAEIDSLWEI SKQIEGHTIC ALGDGAAWPV QGLIRHFRPE LEERMQRFAQ QHQARQAAS

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Macromolecule #2: Mitochondrial complex I, 24 kDa subunit

MacromoleculeName: Mitochondrial complex I, 24 kDa subunit / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sheep (sheep)
Molecular weightTheoretical: 27.373551 KDa
SequenceString: MPVLQYEHLE ECIRWGKHIR NLHKTAVQNG AGGALFVHRD TPKNNPETPF DFTPENYKRI EAIVKNYPEG HKAAAVLPVL DLAQRQNGW LPISAMNKVA EILQVPPMRV YEVATFYTMY NRKPVGKYHI QVCTTTPCML RNSDSILEAI QKKLGIKVGE T TPDKLFTL ...String:
MPVLQYEHLE ECIRWGKHIR NLHKTAVQNG AGGALFVHRD TPKNNPETPF DFTPENYKRI EAIVKNYPEG HKAAAVLPVL DLAQRQNGW LPISAMNKVA EILQVPPMRV YEVATFYTMY NRKPVGKYHI QVCTTTPCML RNSDSILEAI QKKLGIKVGE T TPDKLFTL IEVECLGACV NAPMVQINDN YYEDLTPKDI EEIIDELKAG KIPKPGPRSG RFSCEPAGGL TSLTEPPKGP GF GVQAGL

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Macromolecule #3: NADH:ubiquinone oxidoreductase core subunit S1

MacromoleculeName: NADH:ubiquinone oxidoreductase core subunit S1 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sheep (sheep)
Molecular weightTheoretical: 79.519297 KDa
SequenceString: MLRIPVRKAL VGLSKSSKGC VRTTATAASN LIEVFVDGQS VMVEPGTTVL QACEKVGMQI PRFCYHERLS VAGNCRMCLV EIEKAPKVV AACAMPVMKG WNILTNSEKT KKAREGVMEF LLANHPLDCP ICDQGGECDL QDQSMMFGSD RSRFLEGKRA V EDKNIGPL ...String:
MLRIPVRKAL VGLSKSSKGC VRTTATAASN LIEVFVDGQS VMVEPGTTVL QACEKVGMQI PRFCYHERLS VAGNCRMCLV EIEKAPKVV AACAMPVMKG WNILTNSEKT KKAREGVMEF LLANHPLDCP ICDQGGECDL QDQSMMFGSD RSRFLEGKRA V EDKNIGPL VKTIMTRCIQ CTRCIRFASE IAGVDDLGTT GRGNDMQVGT YIEKMFMSEL SGNIIDICPV GALTSKPYAF TA RPWETRK TESIDVMDAV GSNIVVSTRT GEVMRILPRM HEDINEEWIS DKTRFAYDGL KRQRLTEPMV RNEKGLLTHT TWE DALSRV AGMLQSCQGN DVAAIAGGLV DAEALIALKD LLNRVDSDTL CTEEVFPTAG AGTDLRSNYL LNTTIAGVEE ADVV LLVGT NPRFEAPLFN ARIRKSWLHN DLKVALIGSP VDLTYRYDHL GDSPKILQDI ASGSHPFSQV LQEAKKPMVV LGSSA LQRN DGAAILAAVS NIAQKIRTSS GVTGDWKVMN ILHRIASQVA ALDLGYKPGV EAIRKNPPKM LFLLGADGGC VTRQDL PKD CFIVYQGHHG DVGAPIADVI LPGAAYTEKS ATYVNTEGRA QQTKVAVMPP GLAREDWKII RALSEIAGMT LPYDTLD QV RNRLEEVSPN LVRYDDVEGA NYFQQASELS KLVNQQLLAD PLVPPQLTIK DFYMTDSISR ASQTMAKCVK AVTEGAHA V EEPSIC

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Macromolecule #4: Mitochondrial complex I, 49 kDa subunit

MacromoleculeName: Mitochondrial complex I, 49 kDa subunit / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sheep (sheep)
Molecular weightTheoretical: 52.661453 KDa
SequenceString: MAALRALRRL RGAAAQVLRP GAGARLPIQP SRGARQWQPD VEWAEQYGGA VMYPTKETAH WKPPPWNDVD PPKDTLVSNL TLNFGPQHP AAHGVLRLVM ELSGEMVRKC DPHIGLLH(2MR)G TEKLIEYKTY LQALPYFDRL DYVSMMCNEQ AYSLAVE KL LNIQPPPRAQ ...String:
MAALRALRRL RGAAAQVLRP GAGARLPIQP SRGARQWQPD VEWAEQYGGA VMYPTKETAH WKPPPWNDVD PPKDTLVSNL TLNFGPQHP AAHGVLRLVM ELSGEMVRKC DPHIGLLH(2MR)G TEKLIEYKTY LQALPYFDRL DYVSMMCNEQ AYSLAVE KL LNIQPPPRAQ WIRVLFGEIT RLLNHIMAVT THALDIGAMT PFFWMFEERE KMFEFYERVS GARMHAAYVR PGGVHQDL P LGLMDDIYEF SKNFSLRIDE LEEMLTNNRI WRNRTVDIGV VTAEDALNYG FSGVMLRGSG IQWDLRKTQP YDVYDQVEF DVPIGSRGDC YDRYLCRVEE MRQSIRIISQ CLNKMPPGEI KVDDAKVSPP KRAEMKTSME SLIHHFKLYT EGYQVPPGAT YTAIEAPKG EFGVYLVSDG SSRPYRCKIK APGFAHLAGL DKMSKGHMLA DVVAIIGTQD IVFGEVDR

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Macromolecule #5: NADH:ubiquinone oxidoreductase core subunit S3

MacromoleculeName: NADH:ubiquinone oxidoreductase core subunit S3 / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sheep (sheep)
Molecular weightTheoretical: 30.38457 KDa
SequenceString: PVKMAAAAAR GCWQRLVGSA APARVAGRPS VLLLPVRRES ASADTRPTVR PRNDVAHKQL SAFGEYVAEI LPKYVQQVQV SCFSELEIC IHPDGVIPVL TFLRDHSNAQ FKSLADLTAV DIPTRQNRFE IVYNLLSLRF NSRIRVKTYT DELTPVESSV S VYKAANWY ...String:
PVKMAAAAAR GCWQRLVGSA APARVAGRPS VLLLPVRRES ASADTRPTVR PRNDVAHKQL SAFGEYVAEI LPKYVQQVQV SCFSELEIC IHPDGVIPVL TFLRDHSNAQ FKSLADLTAV DIPTRQNRFE IVYNLLSLRF NSRIRVKTYT DELTPVESSV S VYKAANWY EREIWDMFGV FFANHPDLRR ILTDYGFEGH PFRKDFPLSG YVELRYDDEV KRVVAEPVEL AQEFRKFDLN SP WEAFPAY RQPPESLKLE AGDKKPEAK

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Macromolecule #6: Mitochondrial complex I, PSST subunit

MacromoleculeName: Mitochondrial complex I, PSST subunit / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sheep (sheep)
Molecular weightTheoretical: 24.6229 KDa
SequenceString: MLPLKFPGRG GAAPRLFHPI LAVRSGMGAA LQVRGVHSSM AADSPSSTQP AVSQARAVVP KPAALPSSRG EYVVAKLDDL INWARRSSL WPMTFGLACC AVEMMHMAAP RYDMDRFGVV FRASPRQSDV MIVAGTLTNK MAPALRKVYD QMPEPRYVVS M GSCANGGG ...String:
MLPLKFPGRG GAAPRLFHPI LAVRSGMGAA LQVRGVHSSM AADSPSSTQP AVSQARAVVP KPAALPSSRG EYVVAKLDDL INWARRSSL WPMTFGLACC AVEMMHMAAP RYDMDRFGVV FRASPRQSDV MIVAGTLTNK MAPALRKVYD QMPEPRYVVS M GSCANGGG YYHYSYSVVR GCDRIVPVDI YVPGCPPTAE ALLYGILQLQ KKIKREKRLR IWYRR

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Macromolecule #7: Mitochondrial complex I, TYKY subunit

MacromoleculeName: Mitochondrial complex I, TYKY subunit / type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sheep (sheep)
Molecular weightTheoretical: 24.496121 KDa
SequenceString: MRKPKMRCLT MPVLLRALAQ AQAARAGHAS GRGLHSSAVA ATYKYVNLRE PSMDMKSVTD RAAQTLLWTE LIRGLGMTLS YLFREPATI NYPFEKGPLS PRFRGEHALR RYPSGEERCI ACKLCEAVCP AQAITIEAEP RADGSRRTTR YDIDMTKCIY C GFCQEACP ...String:
MRKPKMRCLT MPVLLRALAQ AQAARAGHAS GRGLHSSAVA ATYKYVNLRE PSMDMKSVTD RAAQTLLWTE LIRGLGMTLS YLFREPATI NYPFEKGPLS PRFRGEHALR RYPSGEERCI ACKLCEAVCP AQAITIEAEP RADGSRRTTR YDIDMTKCIY C GFCQEACP VDAIVEGPNF EFSTETHEEL LYNKEKLLNN GDKWEAEIAA NIQADYLYR

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Macromolecule #8: Mitochondrial complex I, 10 kDa subunit

MacromoleculeName: Mitochondrial complex I, 10 kDa subunit / type: protein_or_peptide / ID: 8 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sheep (sheep)
Molecular weightTheoretical: 11.916529 KDa
SequenceString:
MAASLLLRQG RPGTLKTVLL EAGVFRGLAP AVSLSAESGK NEKGLPPNPK KQSPPKKPAS AAPTEPFDNT TYKNLQHHDY STYTFLDLN LDLSKFRMPQ PSSGRESPRH

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Macromolecule #9: Mitochondrial complex I, 13 kDa subunit

MacromoleculeName: Mitochondrial complex I, 13 kDa subunit / type: protein_or_peptide / ID: 9 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sheep (sheep)
Molecular weightTheoretical: 13.457175 KDa
SequenceString:
MAAAVTFLRL LGRGGAVTRG LPGGARCFGV RTSPTGEKVT HTGQVYDDED YRRVRFVGRQ KEVNENFAID LIAEQPVSQV GSRVISCDG GGGALGHPRV YINLDKETKT GTCGYCGLQF RQQHH

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Macromolecule #10: NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial
type: protein_or_peptide / ID: 10 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sheep (sheep)
Molecular weightTheoretical: 19.381994 KDa
SequenceString:
MSVALRQALW GRRVGTVAAV SVSKVSTRSL STSTWRLAQD QTRDTQLITV DEKLDITTLT GVPEEHIKTR KARIFVPARN NMQSGVNNT KKWKMEFDTR ERWENPLMGW ASTADPLSNL VLTFSTKEDA IAFAEKNGWS YDVEERKVPK PKSKSYGANF S WNKRTRVS TK

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Macromolecule #11: NADH:ubiquinone oxidoreductase subunit A9

MacromoleculeName: NADH:ubiquinone oxidoreductase subunit A9 / type: protein_or_peptide / ID: 11 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sheep (sheep)
Molecular weightTheoretical: 43.02559 KDa
SequenceString: MAAAVHLRVV RVLPMSRSSV PALAASVFHS PPQRQLHHAV IPHGKGGRSS VSGIVATVFG ATGFLGRYLV NHLGRMGSQV IVPYRCEPY DTMHLRPMGD LGQIIFMDWN GRDKDSIRRA VEHSNVVINL VGREWETKNF DFEDVFVKIP QAIAQVSKEA G VEKFIHIS ...String:
MAAAVHLRVV RVLPMSRSSV PALAASVFHS PPQRQLHHAV IPHGKGGRSS VSGIVATVFG ATGFLGRYLV NHLGRMGSQV IVPYRCEPY DTMHLRPMGD LGQIIFMDWN GRDKDSIRRA VEHSNVVINL VGREWETKNF DFEDVFVKIP QAIAQVSKEA G VEKFIHIS HLNADIKSSS KYLRNKAVGE KEVRETFPEA TIIKPADIFG REDRFLNYFA NIRWFGGVPL ISLGKKTVKQ PV YIVDVTK GIINAIKDPD ARGKTFAFVG PNRYLLFDLV QYVFAVAHRP FLPYPMPHFA YRWIGRLFEI SPFEPWTTRD KVE RIHTTD RTLPHLPGLE DLGVQATPLE LKAIEVLRRH RTYRWLSSEI EDVQPAKTVP ASGP

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Macromolecule #12: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2
type: protein_or_peptide / ID: 12 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sheep (sheep)
Molecular weightTheoretical: 11.097824 KDa
SequenceString:
MAAAAAIRGV RGKLGLREIR IHLCQRSPGS QGVRDFIEKR YVELKKANPD LPILIRECSD VQPKLWARYA FGQEKNVSLN NFSADQVTR ALENVLSSKA

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Macromolecule #13: Mitochondrial complex I, B13 subunit

MacromoleculeName: Mitochondrial complex I, B13 subunit / type: protein_or_peptide / ID: 13 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sheep (sheep)
Molecular weightTheoretical: 13.287505 KDa
SequenceString:
MAGLLKKTTG LVGLAVCETP HERLKILYTK ILDVLGHIPK NAAYRKYTEQ ITNEKLSIVK AEPDVKKLEE QLQGGQIEEV ILQAENELS LARKMIQWKP WEPLVEEPPA SQWKWPI

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Macromolecule #14: NADH:ubiquinone oxidoreductase subunit A6

MacromoleculeName: NADH:ubiquinone oxidoreductase subunit A6 / type: protein_or_peptide / ID: 14 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sheep (sheep)
Molecular weightTheoretical: 16.302812 KDa
SequenceString:
NGVELGSDFL SKMAASGLRQ AAVAASTSVK PIFSRDMNEA KRRVRELYRA WYREVPNTVH LFQLDISVKQ GRDKVREMFK KNAHVTDPR VVDLLVIKGK MELEETINVW KQRTHVMRFF HETEAPRPKD FLSKFYVGHD P

+
Macromolecule #15: Mitochondrial complex I, B14.5a subunit

MacromoleculeName: Mitochondrial complex I, B14.5a subunit / type: protein_or_peptide / ID: 15 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sheep (sheep)
Molecular weightTheoretical: 12.701613 KDa
SequenceString:
KM(AYA)SATRLIQ GLRNWASGRD LQAKLQLRYQ EISKRTQPPP KLPVGPSHRL SNNYYCARDG RREAMPPSIV MSSQKV LVA GKPAESSAVA ASEKKAVSPA PPIKRWELSQ DEPYL

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

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12
type: protein_or_peptide / ID: 16 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sheep (sheep)
Molecular weightTheoretical: 17.115508 KDa
SequenceString:
MELLQVLKRG LQQVSGHGGL RGYLRVLFRA NDVRVGTLVG EDKYGNKYYE DNKQFFGRHR WVIYTTEMNG KNTFWDVDGS MVPPEWHRW LHCMTDDPPT VKPPTARKFI WTNHKFNLSG TPQQYVPYST TRKKIQEWVP PSTPYK

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Macromolecule #17: Acyl carrier protein

MacromoleculeName: Acyl carrier protein / type: protein_or_peptide / ID: 17 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sheep (sheep)
Molecular weightTheoretical: 17.608199 KDa
SequenceString:
VEVKDFYTTN YQTAVSFSPL GPMPSMALMA VSLSGANVPK SGGRPEESRV PVLTQRKVPG RVTPLCRQYS DAPPLTLEGI KDRVLYVLK LYDKIDPEKL SVNSHFMKDL GLDSLDQVEI IMAMEDEFGF EIPDIDAEKL MCPQEIVDYI ADKKDVYE

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Macromolecule #18: Mitochondrial complex I, B16.6 subunit

MacromoleculeName: Mitochondrial complex I, B16.6 subunit / type: protein_or_peptide / ID: 18 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sheep (sheep)
Molecular weightTheoretical: 16.766461 KDa
SequenceString:
MAASKVKQDM PPVGGYGPID YKRNLPRRGL SGYSMFAVGI GALLFGYWSM MRWNRERRRL QIEDFEARIA LMPLLQAEKD RRVLQMLRE NLEEEATIMK DVPGWKVGES VFHTTRWVTP MMGELYGLRT GEEILSSTYG FIWYT

+
Macromolecule #19: IRON/SULFUR CLUSTER

MacromoleculeName: IRON/SULFUR CLUSTER / type: ligand / ID: 19 / 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 #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: 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE

MacromoleculeName: 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE / type: ligand / ID: 21 / Number of copies: 1 / Formula: NAI
Molecular weightTheoretical: 665.441 Da
Chemical component information

ChemComp-NAI:
1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE / Nicotinamide adenine dinucleotide

+
Macromolecule #22: FE2/S2 (INORGANIC) CLUSTER

MacromoleculeName: FE2/S2 (INORGANIC) CLUSTER / type: ligand / ID: 22 / Number of copies: 2 / Formula: FES
Molecular weightTheoretical: 175.82 Da
Chemical component information

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

+
Macromolecule #23: POTASSIUM ION

MacromoleculeName: POTASSIUM ION / type: ligand / ID: 23 / Number of copies: 1 / Formula: K
Molecular weightTheoretical: 39.098 Da

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Macromolecule #24: 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE

MacromoleculeName: 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE / type: ligand / ID: 24 / Number of copies: 2 / Formula: PC1
Molecular weightTheoretical: 790.145 Da
Chemical component information

ChemComp-PC1:
1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE / phospholipid*YM / Phosphatidylcholine

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Macromolecule #25: 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOETHANOLAMINE

MacromoleculeName: 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOETHANOLAMINE / type: ligand / ID: 25 / Number of copies: 2 / Formula: 3PE
Molecular weightTheoretical: 748.065 Da

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Macromolecule #26: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 26 / Number of copies: 1 / Formula: ZN
Molecular weightTheoretical: 65.409 Da

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Macromolecule #27: NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE

MacromoleculeName: NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
type: ligand / ID: 27 / 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 #28: S-[2-({N-[(2S)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-b...

MacromoleculeName: S-[2-({N-[(2S)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl] tetradecanethioate
type: ligand / ID: 28 / Number of copies: 1 / Formula: ZMP
Molecular weightTheoretical: 568.704 Da
Chemical component information

ChemComp-ZMP:
S-[2-({N-[(2S)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl] tetradecanethioate

+
Macromolecule #29: CARDIOLIPIN

MacromoleculeName: CARDIOLIPIN / type: ligand / ID: 29 / Number of copies: 1 / Formula: CDL
Molecular weightTheoretical: 1.464043 KDa
Chemical component information

ChemComp-CDL:
CARDIOLIPIN / phospholipid*YM / Cardiolipin

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Macromolecule #30: water

MacromoleculeName: water / type: ligand / ID: 30 / Number of copies: 1472 / Formula: HOH
Molecular weightTheoretical: 18.015 Da
Chemical component information

ChemComp-HOH:
WATER / Water

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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

Concentration3 mg/mL
BufferpH: 7.4
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV

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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 / Cs: 2.7 mm
Image recordingFilm or detector model: FEI FALCON III (4k x 4k) / Detector mode: INTEGRATING / Average electron dose: 100.0 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionSoftware - Name: CTFFIND (ver. 4.15)
Startup modelType of model: PDB ENTRY
PDB model - PDB ID:

5lnk

Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 3.0)
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 3.0)
Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 2.3 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 3.0) / Number images used: 315484
FSC plot (resolution estimation)

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Atomic model buiding 1

Initial modelPDB ID:

5lnk

RefinementSpace: REAL / Protocol: FLEXIBLE FIT / Overall B value: 38 / Target criteria: Correlation coefficient
Output model

PDB-6zk9:
Peripheral domain of open complex I during turnover

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