[English] 日本語
Yorodumi
- EMDB-42231: In-situ structure of typeA supercomplex in respiratory chain ( lo... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: EMDB / ID: EMD-42231
TitleIn-situ structure of typeA supercomplex in respiratory chain ( local refined map focused on CI iron-sulfur cluster regions )
Map data
Sample
  • Complex: In-situ structure of typeA supercomplex in respiratory chain ( local refined map focused on CI iron-sulfur cluster regions )
    • Protein or peptide: x 12 types
  • Ligand: x 2 types
Keywordsin-situ cryo-EM structure / mammalian / mitochondria / respiratory supercomplex / proton pumping / membrane protein / electron transport
Function / homology
Function and homology information


RHOG GTPase cycle / Complex I biogenesis / Respiratory electron transport / Mitochondrial protein degradation / ubiquinone-6 biosynthetic process / cellular respiration / oxidoreductase activity, acting on NAD(P)H / NADH:ubiquinone reductase (H+-translocating) / apoptotic mitochondrial changes / mitochondrial respiratory chain complex I ...RHOG GTPase cycle / Complex I biogenesis / Respiratory electron transport / Mitochondrial protein degradation / ubiquinone-6 biosynthetic process / cellular respiration / oxidoreductase activity, acting on NAD(P)H / NADH:ubiquinone reductase (H+-translocating) / apoptotic mitochondrial changes / mitochondrial respiratory chain complex I / mitochondrial electron transport, NADH to ubiquinone / mitochondrial respiratory chain complex I assembly / NADH dehydrogenase (ubiquinone) activity / electron transport coupled proton transport / quinone binding / ATP metabolic process / negative regulation of intrinsic apoptotic signaling pathway / aerobic respiration / response to cAMP / reactive oxygen species metabolic process / regulation of mitochondrial membrane potential / electron transport chain / regulation of protein phosphorylation / brain development / mitochondrial intermembrane space / negative regulation of cell growth / NAD binding / positive regulation of fibroblast proliferation / 4 iron, 4 sulfur cluster binding / response to oxidative stress / mitochondrial inner membrane / nuclear body / protein-containing complex binding / mitochondrion / metal ion binding
Similarity search - Function
NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial / Zinc finger, CHCC-type / Zinc-finger 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] 1 alpha subcomplex subunit 12 / NADH ubiquinone oxidoreductase subunit NDUFA12 / NADH dehydrogenase [ubiquinone] (complex I), alpha subcomplex, subunit 6 ...NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial / Zinc finger, CHCC-type / Zinc-finger 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] 1 alpha subcomplex subunit 12 / NADH ubiquinone oxidoreductase subunit NDUFA12 / 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, 30kDa subunit, conserved site / Respiratory chain NADH dehydrogenase 30 Kd subunit signature. / Complex 1 LYR protein domain / Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 1. / Complex 1 protein (LYR family) / 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 / NADH:ubiquinone/plastoquinone oxidoreductase, chain 3 / NADH:ubiquinone oxidoreductase, subunit 3 superfamily / NADH-ubiquinone/plastoquinone oxidoreductase, chain 3 / NADH:ubiquinone oxidoreductase, subunit 1, conserved site / Respiratory-chain NADH dehydrogenase subunit 1 signature 1. / Respiratory-chain NADH dehydrogenase subunit 1 signature 2. / NADH:ubiquinone oxidoreductase, subunit 1/F420H2 oxidoreductase subunit H / NADH dehydrogenase / NADH:ubiquinone oxidoreductase, subunit G, iron-sulphur binding / His(Cys)3-ligated-type [4Fe-4S] domain profile. / 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 / 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 / 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 / NAD(P)-binding domain superfamily
Similarity search - Domain/homology
NADH-ubiquinone oxidoreductase chain 1 / NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial / NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6 / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12 / NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial / NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial / NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial / NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial ...NADH-ubiquinone oxidoreductase chain 1 / NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial / NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6 / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12 / NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial / NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial / NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial / NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial / NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial / NADH-ubiquinone oxidoreductase chain 3
Similarity search - Component
Biological speciesSus scrofa (pig)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.0 Å
AuthorsZheng W / Zhang K / Zhu J
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)1R35GM142959 United States
CitationJournal: Nature / Year: 2024
Title: High-resolution in situ structures of mammalian respiratory supercomplexes.
Authors: Wan Zheng / Pengxin Chai / Jiapeng Zhu / Kai Zhang /
Abstract: Mitochondria play a pivotal part in ATP energy production through oxidative phosphorylation, which occurs within the inner membrane through a series of respiratory complexes. Despite extensive in ...Mitochondria play a pivotal part in ATP energy production through oxidative phosphorylation, which occurs within the inner membrane through a series of respiratory complexes. Despite extensive in vitro structural studies, determining the atomic details of their molecular mechanisms in physiological states remains a major challenge, primarily because of loss of the native environment during purification. Here we directly image porcine mitochondria using an in situ cryo-electron microscopy approach. This enables us to determine the structures of various high-order assemblies of respiratory supercomplexes in their native states. We identify four main supercomplex organizations: IIIIIV, IIIIIV, IIIIIV and IIIIIV, which potentially expand into higher-order arrays on the inner membranes. These diverse supercomplexes are largely formed by 'protein-lipids-protein' interactions, which in turn have a substantial impact on the local geometry of the surrounding membranes. Our in situ structures also capture numerous reactive intermediates within these respiratory supercomplexes, shedding light on the dynamic processes of the ubiquinone/ubiquinol exchange mechanism in complex I and the Q-cycle in complex III. Structural comparison of supercomplexes from mitochondria treated under different conditions indicates a possible correlation between conformational states of complexes I and III, probably in response to environmental changes. By preserving the native membrane environment, our approach enables structural studies of mitochondrial respiratory supercomplexes in reaction at high resolution across multiple scales, from atomic-level details to the broader subcellular context.
History
DepositionOct 5, 2023-
Header (metadata) releaseJun 19, 2024-
Map releaseJun 19, 2024-
UpdateJun 19, 2024-
Current statusJun 19, 2024Processing site: RCSB / Status: Released

-
Structure visualization

Supplemental images

emd_42231.png

Downloads & links

-
Map

FileDownload / File: emd_42231.map.gz / Format: CCP4 / Size: 67 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.42 Å/pix.
x 260 pix.
= 108.16 Å		0.42 Å/pix.
x 260 pix.
= 108.16 Å		0.42 Å/pix.
x 260 pix.
= 108.16 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.416 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.07
Minimum - Maximum-1.1929859 - 1.3692126
Average (Standard dev.)0.0010155824 (±0.067252524)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions260260260
Spacing260260260
CellA=B=C: 108.16 Å
α=β=γ: 90.0 °

-
Supplemental data

-
Half map: #1

Fileemd_42231_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

-
Half map: #2

Fileemd_42231_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

-
Sample components

+
Entire : In-situ structure of typeA supercomplex in respiratory chain ( lo...

EntireName: In-situ structure of typeA supercomplex in respiratory chain ( local refined map focused on CI iron-sulfur cluster regions )
Components
  • Complex: In-situ structure of typeA supercomplex in respiratory chain ( local refined map focused on CI iron-sulfur cluster regions )
    • Protein or peptide: NADH-ubiquinone oxidoreductase chain 3
    • Protein or peptide: NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial
    • Protein or peptide: NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
    • Protein or peptide: NADH-ubiquinone oxidoreductase chain 1
    • Protein or peptide: NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, 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 6
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12
  • Ligand: IRON/SULFUR CLUSTERIron–sulfur cluster
  • Ligand: ZINC ION

+
Supramolecule #1: In-situ structure of typeA supercomplex in respiratory chain ( lo...

SupramoleculeName: In-situ structure of typeA supercomplex in respiratory chain ( local refined map focused on CI iron-sulfur cluster regions )
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#12
Source (natural)Organism: Sus scrofa (pig)

+
Macromolecule #1: NADH-ubiquinone oxidoreductase chain 3

MacromoleculeName: NADH-ubiquinone oxidoreductase chain 3 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 12.998448 KDa
SequenceString:
MNIMLTLLTN VTLASLLVLI AFWLPQLNAY SEKTSPYECG FDPMGSARLP FSMKFFLVAI TFLLFDLEIA LLLPLPWASQ TNNLKTMLT MALFLLILLA ASLAYEWTQK GLEWAE

UniProtKB: NADH-ubiquinone oxidoreductase chain 3

+
Macromolecule #2: NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial
type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 28.500184 KDa
SequenceString: MRNVSTQVPV SAHRPSRFGQ RPRIPGALQR TDRRGCLKAE AEMAALAASG LLRPILALRS SMGAAVQVRF VHPSAATDSP SSSQPAVSQ AGAVVSKPTT LPSSRGEYVV AKLDDLVNWA RRSSLWPMTF GLACCAVEMM HMAAPRYDMD RFGVVFRASP R QSDVMIVA ...String:
MRNVSTQVPV SAHRPSRFGQ RPRIPGALQR TDRRGCLKAE AEMAALAASG LLRPILALRS SMGAAVQVRF VHPSAATDSP SSSQPAVSQ AGAVVSKPTT LPSSRGEYVV AKLDDLVNWA RRSSLWPMTF GLACCAVEMM HMAAPRYDMD RFGVVFRASP R QSDVMIVA GTLTNKMAPA LRKVYDQMPE PRYVVSMGSC ANGGGYYHYS YSVVRGCDRI VPVDIYVPGC PPTAEALLYG IL QLQRKIK REKRLRIWYR R

UniProtKB: NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial

+
Macromolecule #3: NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial
type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 30.154318 KDa
SequenceString: MAAAAAARGC WRGLVGPAAV ARVSGRPSVL LLPVRKESAA ADTRPTIRPR NDVVHKQLSA FGQYVAEILP KYVQQVQVSC FNELEIFIH PDGVIPVLTF LRDHTNAQFK SLADLTAVDV PTRQNRFEIV YNLLSLRFNS QIRVKTYTDE LTPIESSVTV Y KAANWYER ...String:
MAAAAAARGC WRGLVGPAAV ARVSGRPSVL LLPVRKESAA ADTRPTIRPR NDVVHKQLSA FGQYVAEILP KYVQQVQVSC FNELEIFIH PDGVIPVLTF LRDHTNAQFK SLADLTAVDV PTRQNRFEIV YNLLSLRFNS QIRVKTYTDE LTPIESSVTV Y KAANWYER EIWDMFGVFF ANHPDLRRIL TGYGFEGHPF RKDFPLSGYV ELRYDDEVKR VVAEPVELAQ EFRKFDLNSP WE AFPAYRQ PPEDLKLEAG DKKPETK

UniProtKB: NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial

+
Macromolecule #4: NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial
type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 54.168074 KDa
SequenceString: MAALRALCSL RGVAAQVLRP GAGARLPIQP SRGARQWQPD VEWAEQFGGA VMYPTKETAH WKPPPWNGNY YWPNYFPLLS DVDPPKDTL VSNLTLNFGP QHPAAHGVLR LVMELSGEMV RKCDPHIGLL HRGTEKLIEY KTYLQALPYF DRLDYVSMMC N EQAYSLAV ...String:
MAALRALCSL RGVAAQVLRP GAGARLPIQP SRGARQWQPD VEWAEQFGGA VMYPTKETAH WKPPPWNGNY YWPNYFPLLS DVDPPKDTL VSNLTLNFGP QHPAAHGVLR LVMELSGEMV RKCDPHIGLL HRGTEKLIEY KTYLQALPYF DRLDYVSMMC N EQAYSLAV EKLLNIQPPP RAQWIRVLFG EITRLLNHIM AVTTHALDIG AMTPFFWMFE EREKMFEFYE RVSGARMHAA YI RPGGVHQ DLPLGLLDDI YEFSKNFSFR IDELEEMLTN NRIWRNRTVD IGVVTAEDAL NYGFSGVMLR GSGIQWDLRK TQP YDVYDQ VEFDVPIGSR GDCYDRYLCR VEEMRQSLRI ISQCLNKMPP GEIKVDDAKV SPPKRAEMKT SMESLIHHFK LYTE GYQVP PGATYTAIEA PKGEFGVYLV SDGSSRPYRC KIKAPGFAHL AGLDKMSKGH MLADVVAIIG TQDIVFGEVD R

UniProtKB: NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial

+
Macromolecule #5: NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial

MacromoleculeName: NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 79.627398 KDa
SequenceString: MLRIPVTRAL IGLSKSPKGC VRTTATAASN LIEVFVDGQS VMVEPGTTVL QACEKVGMQI PRFCYHERLS VAGNCRMCLV EIEKAPKVV AACAMPVMKG WNILTNSEKS KKAREGVMEF LLANHPLDCP ICDQGGECDL QDQSMMFGSD RSRFLEGKRA V EDKNIGPL ...String:
MLRIPVTRAL IGLSKSPKGC VRTTATAASN LIEVFVDGQS VMVEPGTTVL QACEKVGMQI PRFCYHERLS VAGNCRMCLV EIEKAPKVV AACAMPVMKG WNILTNSEKS KKAREGVMEF LLANHPLDCP ICDQGGECDL QDQSMMFGSD RSRFLEGKRA V EDKNIGPL VKTIMTRCIQ CTRCIRFASE IAGVDDLGTT GRGNDMQVGT YIEKMFMSEL SGNIIDICPV GALTSKPYAF TA RPWETRK TESIDVMDAV GSNIVVSTRT GEVMRILPRM HEDINEEWIS DKTRFAYDGL KRQRLTQPMI RNEKGLLTYT TWE DALSRV AGMLQSFQGN DVAAIAGGLV DAEALVALKD LLNRVDSDSL CTEEVFPTAG AGTDLRSNYL LNTTIAGVEE ADVI LLVGT NPRFEAPLFN ARIRKSWLHN DLKVALIGSP VDLTYRYDHL GDSPKILQDI ASGNHPFSQI LKEAKKPMVV LGSSA LQRS DGTAILAAVS NIAQNIRLSS GVTGDWKVMN ILHRIASQVA ALDLGYKPGV EAIRKNPPKV LFLLGADGGC ITRQDL PKD CFIIYQGHHG DVGAPMADVI LPGAAYTEKS ATYVNTEGRA QQTKVAVTPP GLAREDWKII RALSEIAGMT LPYDTLD QV RSRLEEVSPN LVRYDDVEGA NYFQQANELS KLVNQQLLAD PLVPPQLTIK DFYMTDSISR ASQTMAKCVK AVTEGIQA V EEPSIC

UniProtKB: NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial

+
Macromolecule #6: NADH-ubiquinone oxidoreductase chain 1

MacromoleculeName: NADH-ubiquinone oxidoreductase chain 1 / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 35.591426 KDa
SequenceString: MFMINILSLI IPILLAVAFL TLVERKVLGY MQLRKGPNVV GPYGLLQPIA DALKLVTKEP LRPGTSSISM FIIAPILGLS LALTMWVPL PMPYPLINMN LGVLFMLAMS SLAVYSILWS GWASNSKYAL IGALRAVAQT ISYEVTLAII LLSVLLMNGS Y TLSTLITT ...String:
MFMINILSLI IPILLAVAFL TLVERKVLGY MQLRKGPNVV GPYGLLQPIA DALKLVTKEP LRPGTSSISM FIIAPILGLS LALTMWVPL PMPYPLINMN LGVLFMLAMS SLAVYSILWS GWASNSKYAL IGALRAVAQT ISYEVTLAII LLSVLLMNGS Y TLSTLITT QEHIWMIFTS WPLAMMWFIS TLAETNRAPF DLTEGESELV SGFNVEYAAG PFAMFFMAEY ANIIMMNAFT AI LFLGASH DPHTPELYTI NFVLKTLALT ITFLWIRASY PRFRYDQLMH LLWKSFLPLT LALCMWHISL PIMTASIPPQ S

UniProtKB: NADH-ubiquinone oxidoreductase chain 1

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

MacromoleculeName: NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 27.135039 KDa
SequenceString: MEASQECRLR LSVDRPPPHG KERQRFKMRC LSTPMLLRAL AQAQAAHAGH PSARTLHSSA VAATYKFVNM REPSMDMKSV TDRAAQTLL WTELVRGLGM TLSYLFREPA TINYPFEKGP LSPRFRGEHA LRRYPSGEER CIACKLCEAV CPAQAITIEA E PRADGSRR ...String:
MEASQECRLR LSVDRPPPHG KERQRFKMRC LSTPMLLRAL AQAQAAHAGH PSARTLHSSA VAATYKFVNM REPSMDMKSV TDRAAQTLL WTELVRGLGM TLSYLFREPA TINYPFEKGP LSPRFRGEHA LRRYPSGEER CIACKLCEAV CPAQAITIEA E PRADGSRR TTRYDIDMTK CIYCGFCQEA CPVDAIVEGP NFEFSTETHE ELLYNKEKLL NNGDKWEAEI AANIQADYLY R

UniProtKB: NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial

+
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: Sus scrofa (pig)
Molecular weightTheoretical: 42.606324 KDa
SequenceString: MAAAVHPRVV RAVPMSRSCL AAVATSVSYG PPQRQLHHAL IPHGKGGRSS VSGIVATVFG ATGFLGRYVV NHLGRMGSQV IVPYRCEPY DTMHLRPMGD LGQIIFMEWN GKDKDSIRKV VEHSNVVINL VGREWETKNF DFEDVFVKIP HAIAQVSKEA G VEKLIHIS ...String:
MAAAVHPRVV RAVPMSRSCL AAVATSVSYG PPQRQLHHAL IPHGKGGRSS VSGIVATVFG ATGFLGRYVV NHLGRMGSQV IVPYRCEPY DTMHLRPMGD LGQIIFMEWN GKDKDSIRKV VEHSNVVINL VGREWETKNF DFEDVFVKIP HAIAQVSKEA G VEKLIHIS HLNADIKSPS RYLRSKAVGE KEVRAAFPEA TIIKPSDIFG REDRFLNYFA SMRWFGGVPL ISLGKETVKQ PV YIVDVSK GIINAIKDPD AKGKTFAFVG PNRYLLFDLV QYIFAVAYRP FLPYPLPHFA YRWVGRLFEV SPFEPWTTRD KVE RVHMSD MTLPHLPGLE DLGIQATPLE LKAIEVLRRH RTYRWLTSEM EDVKPAKTVN I

UniProtKB: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial

+
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: Sus scrofa (pig)
Molecular weightTheoretical: 19.746514 KDa
SequenceString:
MAAVSMSVAL KQALWGRRAA AVGAVSVSKV PTRLLSTSTW RLAQDQTQDT QLIAVDEKLD ITTLTGVPEE HIKTRKVRIF VPARNNMQS GVNNTKKWKM EFDTRERWEN PLMGWSSTAD PLSNLVLTFS TKEDAVAFAE KNGWSFDVEE RKVPKPKSKS Y GANFSWNK RTRVSTK

UniProtKB: NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial

+
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: Sus scrofa (pig)
Molecular weightTheoretical: 13.34895 KDa
SequenceString:
MAAVTFLRLL GRSGAGARNL LGGSRCFGVR TSPTGEKVTH TGQAYDDGDY RRVRFSDRQK EVNENFAIDL IAEQPVSEVG SRVISCDGG GGALGHPRVY INLDKETKTG TCGYCGLQFR QPHH

UniProtKB: NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial

+
Macromolecule #11: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6
type: protein_or_peptide / ID: 11 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 14.953313 KDa
SequenceString:
MAASGLPRAA AAAGTSVKPI FSRDMNEAKR RVRELYRAWY REVPNTVHLF QLDISVKQGR DKVREMFMKN AHVTDPRVVD LLVIKGKME LEETINVWKQ RTHIMRFFHE TEAPRPTDFL SKFYVGHDP

UniProtKB: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6

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

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12
type: protein_or_peptide / ID: 12 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 17.162439 KDa
SequenceString:
MELVQVLRRG LQQVSGHGGL RGYLRVLFRA NDVRVGTLVG EDKYGNKYYE DNKQFFGRHR WVIYTTEMNG RDTFWDVDGS MVPPEWHRW LHCMTDDPPT TKPPTARKYI WTNHKFNVSG TPQQYVPYST TRKKIQEWVP PSTPYK

UniProtKB: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12

+
Macromolecule #13: IRON/SULFUR CLUSTER

MacromoleculeName: IRON/SULFUR CLUSTER / type: ligand / ID: 13 / Number of copies: 3 / Formula: SF4
Molecular weightTheoretical: 351.64 Da
Chemical component information

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

+
Macromolecule #14: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 14 / Number of copies: 1 / Formula: ZN
Molecular weightTheoretical: 65.409 Da

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

BufferpH: 7
VitrificationCryogen name: ETHANE

-
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 / Nominal defocus max: 3.0 µm / Nominal defocus min: 1.3 µm
Image recordingFilm or detector model: GATAN K3 BIOCONTINUUM (6k x 4k) / Average electron dose: 50.0 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

-
Image processing

Startup modelType of model: NONE
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
Final reconstructionResolution.type: BY AUTHOR / Resolution: 2.0 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 60000

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242)：Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more