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- EMDB-51157: Cryo-EM structure of the Toxoplasma gondii respiratory chain comp... -

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Basic information

Entry
Database: EMDB / ID: EMD-51157
TitleCryo-EM structure of the Toxoplasma gondii respiratory chain complex III inhibited by ELQ-300
Map data
Sample
  • Complex: Cytochrome bc1 complex from Toxoplasma gondii
    • Protein or peptide: x 12 types
  • Ligand: x 8 types
Keywordscytochrome bc1 complex / complex III / respiratory chain / ELECTRON TRANSPORT
Function / homology
Function and homology information


quinol-cytochrome-c reductase / mitochondrial processing peptidase / respiratory chain complex III / quinol-cytochrome-c reductase activity / mitochondrial electron transport, ubiquinol to cytochrome c / metalloendopeptidase activity / 2 iron, 2 sulfur cluster binding / electron transfer activity / mitochondrial inner membrane / heme binding ...quinol-cytochrome-c reductase / mitochondrial processing peptidase / respiratory chain complex III / quinol-cytochrome-c reductase activity / mitochondrial electron transport, ubiquinol to cytochrome c / metalloendopeptidase activity / 2 iron, 2 sulfur cluster binding / electron transfer activity / mitochondrial inner membrane / heme binding / mitochondrion / proteolysis / metal ion binding / membrane
Similarity search - Function
Cytochrome b-c1 complex, subunit 6 / Cytochrome b-c1 complex subunit 7 / Cytochrome b-c1 complex subunit 7 superfamily / Ubiquinol-cytochrome C reductase complex 14kD subunit / Cytochrome b-c1 complex subunit 8 superfamily / Ubiquinol-cytochrome C reductase hinge domain / Ubiquinol-cytochrome C reductase hinge domain superfamily / Ubiquinol-cytochrome C reductase hinge protein / Cytochrome b-c1 complex subunit 9 / Cytochrome b-c1 complex subunit 9 superfamily ...Cytochrome b-c1 complex, subunit 6 / Cytochrome b-c1 complex subunit 7 / Cytochrome b-c1 complex subunit 7 superfamily / Ubiquinol-cytochrome C reductase complex 14kD subunit / Cytochrome b-c1 complex subunit 8 superfamily / Ubiquinol-cytochrome C reductase hinge domain / Ubiquinol-cytochrome C reductase hinge domain superfamily / Ubiquinol-cytochrome C reductase hinge protein / Cytochrome b-c1 complex subunit 9 / Cytochrome b-c1 complex subunit 9 superfamily / Ubiquinol-cytochrome C reductase, UQCRX/QCR9 like / Cytochrome c1, transmembrane anchor, C-terminal / : / Ubiquinol-cytochrome c reductase, iron-sulphur subunit / Cytochrome c1 / Cytochrome C1 family / : / Cytochrome b/b6, C-terminal / Cytochrome b(C-terminal)/b6/petD / Cytochrome b/b6 C-terminal region profile. / Peptidase M16, zinc-binding site / Insulinase family, zinc-binding region signature. / Cytochrome b/b6, C-terminal domain superfamily / Cytochrome b/b6/petB / Rieske iron-sulphur protein, C-terminal / Cytochrome b/b6, N-terminal / Cytochrome b/b6-like domain superfamily / Cytochrome b/b6 N-terminal region profile. / Di-haem cytochrome, transmembrane / Rieske iron-sulphur protein / Peptidase M16, C-terminal / Peptidase M16 inactive domain / Peptidase M16, N-terminal / Insulinase (Peptidase family M16) / Metalloenzyme, LuxS/M16 peptidase-like / Rieske [2Fe-2S] domain / Rieske [2Fe-2S] iron-sulphur domain / Rieske [2Fe-2S] iron-sulfur domain profile. / Rieske [2Fe-2S] iron-sulphur domain superfamily / Cytochrome c family profile. / Cytochrome c-like domain / Cytochrome c-like domain superfamily
Similarity search - Domain/homology
Putative peptidase M16, alpha subunit / Uncharacterized protein / Ubiquinol-cytochrome c reductase / Transmembrane protein / Cytochrome b / Putative ubiquinol cytochrome c oxidoreductase / Transmembrane protein / Transmembrane protein / Ubiquinol-cytochrome C family reductase UQCRX/QCR9-like protein / Putative ubiquinol-cytochrome c reductase hinge protein ...Putative peptidase M16, alpha subunit / Uncharacterized protein / Ubiquinol-cytochrome c reductase / Transmembrane protein / Cytochrome b / Putative ubiquinol cytochrome c oxidoreductase / Transmembrane protein / Transmembrane protein / Ubiquinol-cytochrome C family reductase UQCRX/QCR9-like protein / Putative ubiquinol-cytochrome c reductase hinge protein / Putative peptidase M16 family potein / Cytochrome c1, heme protein
Similarity search - Component
Biological speciesToxoplasma gondii (eukaryote)
Methodsingle particle reconstruction / cryo EM / Resolution: 1.8 Å
AuthorsMacLean A / Muhleip A
Funding support United Kingdom, 1 items
OrganizationGrant numberCountry
Wellcome Trust United Kingdom
CitationJournal: Nat Struct Mol Biol / Year: 2025
Title: Structure, assembly and inhibition of the Toxoplasma gondii respiratory chain supercomplex.
Authors: Andrew E MacLean / Shikha Shikha / Mariana Ferreira Silva / Max J Gramelspacher / Aaron Nilsen / Katherine M Liebman / Sovitj Pou / Rolf W Winter / Amit Meir / Michael K Riscoe / J Stone ...Authors: Andrew E MacLean / Shikha Shikha / Mariana Ferreira Silva / Max J Gramelspacher / Aaron Nilsen / Katherine M Liebman / Sovitj Pou / Rolf W Winter / Amit Meir / Michael K Riscoe / J Stone Doggett / Lilach Sheiner / Alexander Mühleip /
Abstract: The apicomplexan mitochondrial electron transport chain is essential for parasite survival and displays a divergent subunit composition. Here we report cryo-electron microscopy structures of an ...The apicomplexan mitochondrial electron transport chain is essential for parasite survival and displays a divergent subunit composition. Here we report cryo-electron microscopy structures of an apicomplexan III-IV supercomplex and of the drug target complex III. The supercomplex structure reveals how clade-specific subunits form an apicomplexan-conserved III-IV interface with a unique, kinked architecture, suggesting that supercomplexes evolved independently in different eukaryotic lineages. A knockout resulting in supercomplex disassembly challenges the proposed role of III-IV in electron transfer efficiency as suggested for mammals. Nevertheless, knockout analysis indicates that III-IV is critical for parasite fitness. The complexes from the model parasite Toxoplasma gondii were inhibited with the antimalarial atovaquone, revealing interactions underpinning species specificity. They were also inhibited with endochin-like quinolone (ELQ)-300, an inhibitor in late-stage preclinical development. Notably, in the apicomplexan binding site, ELQ-300 is flipped compared with related compounds in the mammalian enzyme. On the basis of the binding modes and parasite-specific interactions discovered, we designed more potent ELQs with subnanomolar activity against T. gondii. Our findings reveal critical evolutionary differences in the role of supercomplexes in mitochondrial biology and provide insight into cytochrome b inhibition, informing future drug discovery.
History
DepositionJul 25, 2024-
Header (metadata) releaseJun 18, 2025-
Map releaseJun 18, 2025-
UpdateJun 18, 2025-
Current statusJun 18, 2025Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_51157.png

Downloads & links

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Map

FileDownload / File: emd_51157.map.gz / Format: CCP4 / Size: 421.9 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
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Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.83 Å/pix.
x 480 pix.
= 398.4 Å		0.83 Å/pix.
x 480 pix.
= 398.4 Å		0.83 Å/pix.
x 480 pix.
= 398.4 Å

Surface

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Images are generated by Spider.

Voxel sizeX=Y=Z: 0.83 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.5
Minimum - Maximum-4.441019 - 9.711510000000001
Average (Standard dev.)-0.00077314704 (±0.10702249)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions480480480
Spacing480480480
CellA=B=C: 398.4 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_51157_msk_1.map
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Additional map: density-modified halfmap 2

Fileemd_51157_additional_1.map
Annotationdensity-modified halfmap 2
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Additional map: density-modified halfmap 1

Fileemd_51157_additional_2.map
Annotationdensity-modified halfmap 1
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Additional map: density-modified full map

Fileemd_51157_additional_3.map
Annotationdensity-modified full map
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Half map: #1

Fileemd_51157_half_map_1.map
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Half map: #2

Fileemd_51157_half_map_2.map
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Sample components

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Entire : Cytochrome bc1 complex from Toxoplasma gondii

EntireName: Cytochrome bc1 complex from Toxoplasma gondii
Components
  • Complex: Cytochrome bc1 complex from Toxoplasma gondii
    • Protein or peptide: Cytochrome b
    • Protein or peptide: Cytochrome c1, heme protein
    • Protein or peptide: Putative ubiquinol cytochrome c oxidoreductase
    • Protein or peptide: Putative peptidase M16 family protein
    • Protein or peptide: Alpha-MPP
    • Protein or peptide: Putative ubiquinol-cytochrome c reductase hinge protein
    • Protein or peptide: Ubiquinol-cytochrome c reductase
    • Protein or peptide: QCR8/TGGT1_227910
    • Protein or peptide: Ubiquinol-cytochrome C family reductase UQCRX/QCR9-like protein
    • Protein or peptide: Transmembrane protein
    • Protein or peptide: Transmembrane protein
    • Protein or peptide: Transmembrane protein
  • Ligand: CARDIOLIPIN
  • Ligand: 6-chloranyl-7-methoxy-2-methyl-3-[4-[4-(trifluoromethyloxy)phenoxy]phenyl]-1~{H}-quinolin-4-one
  • Ligand: PROTOPORPHYRIN IX CONTAINING FE
  • Ligand: MAGNESIUM ION
  • Ligand: HEME C
  • Ligand: 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE
  • Ligand: ZINC ION
  • Ligand: water

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Supramolecule #1: Cytochrome bc1 complex from Toxoplasma gondii

SupramoleculeName: Cytochrome bc1 complex from Toxoplasma gondii / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#12
Source (natural)Organism: Toxoplasma gondii (eukaryote) / Strain: RH

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Macromolecule #1: Cytochrome b

MacromoleculeName: Cytochrome b / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Toxoplasma gondii (eukaryote)
Molecular weightTheoretical: 40.79443 KDa
Recombinant expressionOrganism: Toxoplasma gondii (eukaryote)
SequenceString: FMSLFRAHLV FYRCALNLNS SYNFGFLVAM TFVLQIITGI TLAFRYTSEA SCAFASVQHL VREVAAGWEF RMLHATTASF VFLCILIHM TRGLYNWSYS YLTTAWMSGL VLYLLTIATA FLGYVLPWGQ MSFWGATVIT NLLSPIPYLV PWLLGGYYVS D VTLKRFFV ...String:
FMSLFRAHLV FYRCALNLNS SYNFGFLVAM TFVLQIITGI TLAFRYTSEA SCAFASVQHL VREVAAGWEF RMLHATTASF VFLCILIHM TRGLYNWSYS YLTTAWMSGL VLYLLTIATA FLGYVLPWGQ MSFWGATVIT NLLSPIPYLV PWLLGGYYVS D VTLKRFFV LHFILPFIGC IIIVLHIFYL HLNGSSNPAG IDTALKVAFY PHMLMTDAKC LSYLIGLIFL QAAFGLMELS HP DNSIPVN RFVTPLHIVP EWYFLAYYAV LKVIPSKTGG LLVFMSSLIN LGLLSEIRAL NTRMLIRQQF MTRNVVSGWV IIW VYSMIF LIIIGSAIPQ ATYILYGRLA TILYLTTGLV LCLY

UniProtKB: Cytochrome b

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Macromolecule #2: Cytochrome c1, heme protein

MacromoleculeName: Cytochrome c1, heme protein / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Toxoplasma gondii (eukaryote)
Molecular weightTheoretical: 46.025355 KDa
Recombinant expressionOrganism: Toxoplasma gondii (eukaryote)
SequenceString: MGGGGGGALN KLFPGYKDKI WMKVPVQWRQ QMIQHWNKSY EKQVYSESVA LNRTFQARNQ LVLDRLKPSG AYRLPAVDYK RQLSRGTLV EGADFYLPTA QEQQRLARHF EPYSEQEQEE RRKFRFQSIS VYLAVALGAS FVHDYFYQRR PVAWCLEKEP P HPPSYPFW ...String:
MGGGGGGALN KLFPGYKDKI WMKVPVQWRQ QMIQHWNKSY EKQVYSESVA LNRTFQARNQ LVLDRLKPSG AYRLPAVDYK RQLSRGTLV EGADFYLPTA QEQQRLARHF EPYSEQEQEE RRKFRFQSIS VYLAVALGAS FVHDYFYQRR PVAWCLEKEP P HPPSYPFW FKSLFHSHDI PSVRRGYEVY RKVCATCHSM EQLHFRHLVG EVLPEKRVKQ IAAEYDVTDG PNDQGEMYTR PG ILGDAFP SPYPNEEAAR YANGGAYPPD LSLITAARHF GPDYLMALLG GYRDPPEGVE LRPGLYWNVW FPGNAIAMPP PLM DEMIDY EDGTPCNISQ MSKDVVNFLT WATEPTADER KLYGLKCVSA IAIGTVLMTL WWRFYWAMYA TRRIDFGKLK YL

UniProtKB: Cytochrome c1, heme protein

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Macromolecule #3: Putative ubiquinol cytochrome c oxidoreductase

MacromoleculeName: Putative ubiquinol cytochrome c oxidoreductase / type: protein_or_peptide / ID: 3 / Number of copies: 2 / Enantiomer: LEVO / EC number: quinol-cytochrome-c reductase
Source (natural)Organism: Toxoplasma gondii (eukaryote)
Molecular weightTheoretical: 54.869145 KDa
Recombinant expressionOrganism: Toxoplasma gondii (eukaryote)
SequenceString: MRHLARCASR RAVKWTERDS PVANFLRSSS CCPFQLLQAS RAKIQRLRTS ERFRLRSAQK LAPTRFPPFT HGPLFFSLPS RLTVPSSLR SLSAFSAPLS LPFRGTMAFL SSPLFAAKAS LAARVHALGC STTSLTSPLA ARALAASSLS LFSVSPRRHF S VHSHNIRP ...String:
MRHLARCASR RAVKWTERDS PVANFLRSSS CCPFQLLQAS RAKIQRLRTS ERFRLRSAQK LAPTRFPPFT HGPLFFSLPS RLTVPSSLR SLSAFSAPLS LPFRGTMAFL SSPLFAAKAS LAARVHALGC STTSLTSPLA ARALAASSLS LFSVSPRRHF S VHSHNIRP DKHELPASEV PLYYNRFDQA DHPSLWQLEE EQQRKHLDQE VTDVSQLVEP VSSPHQTEGW FKRLRYWHYK ET AEPTFPR TPDLSKGELA AGATVTRTSV WHDPNEPAIV SVSRFAPDNF RAVGFAENVP NPESTNSDSH PDFREYRLGP GSV DRRPFV YFMSASYFFI TASMMRSFLC KWVHYWWVSR DMLAAGTTEV DLRPIQEGMT AVFKWRGKPV FVRHRTAEDI AKAQ ADDAL IGTMKDPQLD SERCPRPQWL INIGVCTHLG CIPTDGGNYG GWFCPCHGSH YDTSGRIRLG PAPSNLELPP TVFLD DHTV KLG

UniProtKB: Putative ubiquinol cytochrome c oxidoreductase

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Macromolecule #4: Putative peptidase M16 family protein

MacromoleculeName: Putative peptidase M16 family protein / type: protein_or_peptide / ID: 4 / Details: Putative peptidase M16 family protein / Number of copies: 2 / Enantiomer: LEVO / EC number: mitochondrial processing peptidase
Source (natural)Organism: Toxoplasma gondii (eukaryote)
Molecular weightTheoretical: 56.986824 KDa
Recombinant expressionOrganism: Toxoplasma gondii (eukaryote)
SequenceString: MMFRFLPRVA SGASSLSVSQ RRLRASFSSS LQSRGFFSAA PAAATAGVSP LARSVDAAIP EEAFNQPPTL TTTLPNGIRV ATQRLPFHQ TATVGVWIDS GSRYDTKETN GAAHFLEHMT FKGTKRRSRI QLEQEIENMG AHLNAYTSRE QTVYYAKAFK K DIPQCVDI ...String:
MMFRFLPRVA SGASSLSVSQ RRLRASFSSS LQSRGFFSAA PAAATAGVSP LARSVDAAIP EEAFNQPPTL TTTLPNGIRV ATQRLPFHQ TATVGVWIDS GSRYDTKETN GAAHFLEHMT FKGTKRRSRI QLEQEIENMG AHLNAYTSRE QTVYYAKAFK K DIPQCVDI LSDILLNSTI DEEAVQMEKH VILREMEEVE RQTEEVIFDR LHTTAFRDSP LGYTILGPEE NIRNMTREHI LE YINRNYT SDRMVVAAAG DVDHKELTAL VEKHFAGLPQ PKRSKIILPT EKPFFCGSEL LHRNDDMGPT AHVAVGFEGV PWK SPDAVT FMLMQAIVGS YRKHDEGIVP GKVSANATVR NVCNKMTVGC ADMFSAFNTC YSDTGLFGFY AQCDEVALEH CVME IMFGI TSLSYAVTDE EVERAKAQLK TQLLGHLDST TAVAEDIGRQ MLAYGRRMPL AEFLKRLEVI DAEEVKRVAW KYLHD AEVA VAGLGPLFGM PQLINLRRAT FWLRY

UniProtKB: Putative peptidase M16 family potein

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Macromolecule #5: Alpha-MPP

MacromoleculeName: Alpha-MPP / type: protein_or_peptide / ID: 5 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Toxoplasma gondii (eukaryote)
Molecular weightTheoretical: 62.238395 KDa
Recombinant expressionOrganism: Toxoplasma gondii (eukaryote)
SequenceString: MNASILFRRN APGVSTCLRR RCLRPAALAA ASASGVSTPA SGVWTPAFQR TEKRFLSGAA LQPKAGPAPE YRRVPFVKED MEKVMEEVP EFKYYYVGKE NTKGNVYEGI PLDQSILEPA DLRDYVPPHS NIQYSKLDNG LRIASMDRGG LTASLGLFVH A GTRFEDVT ...String:
MNASILFRRN APGVSTCLRR RCLRPAALAA ASASGVSTPA SGVWTPAFQR TEKRFLSGAA LQPKAGPAPE YRRVPFVKED MEKVMEEVP EFKYYYVGKE NTKGNVYEGI PLDQSILEPA DLRDYVPPHS NIQYSKLDNG LRIASMDRGG LTASLGLFVH A GTRFEDVT NFGVTHMIQN LAFASTAHLS LLRTVKTIEV LGANAGCVVG REHLVYSAEC LRSHMPLLVP MLTGNVLFPR FL PWELKAC KEKLIMARKR LEHMPDQMVS ELLHTTAWHN NTLGHKLHCT ERSLGHYNPD VIRHYMLQHF SPENMVFVGV NVN HDELCT WLMRAFVDYN AIPPSKRTVA SPVYTGGDVR LETPSPHAHM AIAFETPGGW NGGDLVAYSV LQTILGGGGA FSTG GPGKG MYTRLYLNVL NQNEWVESAM AFNTQYTDSG IFGLYMLADP TKSANAVKVM AEQFGKMGSV TKEELQRAKN SLKSS IFMN LECRGIVMED VGRQLLMSNR VISPQEFCTA IDAVTEADIK RVVDAMYKKP PTVVAYGDVS TVPHYEEVRA ALRAAG VGK

UniProtKB: Putative peptidase M16, alpha subunit

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Macromolecule #6: Putative ubiquinol-cytochrome c reductase hinge protein

MacromoleculeName: Putative ubiquinol-cytochrome c reductase hinge protein
type: protein_or_peptide / ID: 6 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Toxoplasma gondii (eukaryote)
Molecular weightTheoretical: 10.509094 KDa
Recombinant expressionOrganism: Toxoplasma gondii (eukaryote)
SequenceString:
MSYPYYCEFF VKFPNYIPPK DPAERLVDPR QKLEPGCTAR CSLWVNEYDA CTKRVRARTD NKGNCSGQYE ELHVCIDRCV AKDIFKYLK

UniProtKB: Putative ubiquinol-cytochrome c reductase hinge protein

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Macromolecule #7: Ubiquinol-cytochrome c reductase

MacromoleculeName: Ubiquinol-cytochrome c reductase / type: protein_or_peptide / ID: 7 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Toxoplasma gondii (eukaryote)
Molecular weightTheoretical: 26.777564 KDa
Recombinant expressionOrganism: Toxoplasma gondii (eukaryote)
SequenceString: MAQFHREIGK LFASYSNKIT ANSPVQYVPS PPTKGKVRRA LSSALMPVWF KFFRGPLDRW NLAVMAKYLR DHGLMYDDLY SDKEPVFAR ALELLPPDIQ AARFRRLMRG TYLNHLRLYL PVHEQNYDPF IPYMAPYVEE AKFQLQEEEE LLGYHMWEGV W YSGGVTGF ...String:
MAQFHREIGK LFASYSNKIT ANSPVQYVPS PPTKGKVRRA LSSALMPVWF KFFRGPLDRW NLAVMAKYLR DHGLMYDDLY SDKEPVFAR ALELLPPDIQ AARFRRLMRG TYLNHLRLYL PVHEQNYDPF IPYMAPYVEE AKFQLQEEEE LLGYHMWEGV W YSGGVTGF GDKEPGEHFL VALPNLYGAG GSPMQAGGKH FSSHAASAAR ARLATLAQKR LEEAMQQRER QSVSQN

UniProtKB: Ubiquinol-cytochrome c reductase

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Macromolecule #8: QCR8/TGGT1_227910

MacromoleculeName: QCR8/TGGT1_227910 / type: protein_or_peptide / ID: 8 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Toxoplasma gondii (eukaryote)
Molecular weightTheoretical: 14.391657 KDa
Recombinant expressionOrganism: Toxoplasma gondii (eukaryote)
SequenceString:
MAASRLCQYL AGRGQTGLLS LSAPRLGAPK FERKMLGSYP VSPEFEMVWR DRLTAHGGYI QQTISPYQLK FIYPFWHTFF ARCWCKCSA YAWPWVWPGL ITFGLVKKMN HDVEEDIRDH YWY

UniProtKB: Uncharacterized protein

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Macromolecule #9: Ubiquinol-cytochrome C family reductase UQCRX/QCR9-like protein

MacromoleculeName: Ubiquinol-cytochrome C family reductase UQCRX/QCR9-like protein
type: protein_or_peptide / ID: 9 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Toxoplasma gondii (eukaryote)
Molecular weightTheoretical: 15.290577 KDa
Recombinant expressionOrganism: Toxoplasma gondii (eukaryote)
SequenceString:
MHFSGVFLRT SRVFLASESS AAGSKVAKSL PGIRFGNPWR DDYPEWIWKS LRVSRKDKDM FAPFFKLLNA TKLYEYCLKD NRRYCMFVM GVGLVSSWMW SEWWNSVWRR INKGKLYNDV PYVYPEEDE

UniProtKB: Ubiquinol-cytochrome C family reductase UQCRX/QCR9-like protein

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Macromolecule #10: Transmembrane protein

MacromoleculeName: Transmembrane protein / type: protein_or_peptide / ID: 10 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Toxoplasma gondii (eukaryote)
Molecular weightTheoretical: 9.455947 KDa
Recombinant expressionOrganism: Toxoplasma gondii (eukaryote)
SequenceString:
MSRAVYAKLW ASTAQYTQRR HYAWYQIWSR VIPWSVPWGI FAMWMVFPAM PVEYRQALTF GIWQKPNIGT HGPDPADAKK

UniProtKB: Transmembrane protein

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Macromolecule #11: Transmembrane protein

MacromoleculeName: Transmembrane protein / type: protein_or_peptide / ID: 11 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Toxoplasma gondii (eukaryote)
Molecular weightTheoretical: 15.250601 KDa
Recombinant expressionOrganism: Toxoplasma gondii (eukaryote)
SequenceString:
MATHNCLRQT AAQMLGQNAN VFRFFSKSAP SRPSGNVALE SVKNAAVAET ETFAGRANVA AGTGKLEGSL LPPPHIPGIR RAPREPASP KMAGMEGRMP VRLPPEGSRF RQYVDPRADV YFPLTAVLVT LGPLYMFSKA FF

UniProtKB: Transmembrane protein

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Macromolecule #12: Transmembrane protein

MacromoleculeName: Transmembrane protein / type: protein_or_peptide / ID: 12 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Toxoplasma gondii (eukaryote)
Molecular weightTheoretical: 11.723664 KDa
Recombinant expressionOrganism: Toxoplasma gondii (eukaryote)
SequenceString:
MNCPNLPAPE EFVVPVFSAG PPVGKNCFHC GIRLRRGHSS PTYSFPPYCV TMSYGNGTVL MPIVRRVFIG ALVGIYAYAA TDVVLIPGY AQLMQKWKKG SSTPAHGGGH

UniProtKB: Transmembrane protein

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Macromolecule #13: CARDIOLIPIN

MacromoleculeName: CARDIOLIPIN / type: ligand / ID: 13 / Number of copies: 16 / Formula: CDL
Molecular weightTheoretical: 1.464043 KDa
Chemical component information

ChemComp-CDL:
CARDIOLIPIN / phospholipid*YM

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Macromolecule #14: 6-chloranyl-7-methoxy-2-methyl-3-[4-[4-(trifluoromethyloxy)phenox...

MacromoleculeName: 6-chloranyl-7-methoxy-2-methyl-3-[4-[4-(trifluoromethyloxy)phenoxy]phenyl]-1~{H}-quinolin-4-one
type: ligand / ID: 14 / Number of copies: 4 / Formula: A1IJD
Molecular weightTheoretical: 475.844 Da

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Macromolecule #15: PROTOPORPHYRIN IX CONTAINING FE

MacromoleculeName: PROTOPORPHYRIN IX CONTAINING FE / type: ligand / ID: 15 / Number of copies: 4 / Formula: HEM
Molecular weightTheoretical: 616.487 Da
Chemical component information

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE

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Macromolecule #16: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 16 / Number of copies: 2 / Formula: MG
Molecular weightTheoretical: 24.305 Da

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Macromolecule #17: HEME C

MacromoleculeName: HEME C / type: ligand / ID: 17 / Number of copies: 2 / Formula: HEC
Molecular weightTheoretical: 618.503 Da
Chemical component information

ChemComp-HEC:
HEME C

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Macromolecule #18: 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE

MacromoleculeName: 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE / type: ligand / ID: 18 / 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

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Macromolecule #19: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 19 / Number of copies: 2 / Formula: ZN
Molecular weightTheoretical: 65.409 Da

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Macromolecule #20: water

MacromoleculeName: water / type: ligand / ID: 20 / Number of copies: 683 / Formula: HOH
Molecular weightTheoretical: 18.015 Da
Chemical component information

ChemComp-HOH:
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

BufferpH: 7.4
VitrificationCryogen name: ETHANE / Chamber humidity: 100 %

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 36.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 2.7 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.4000000000000001 µm / Nominal defocus min: 0.4 µm
Sample stageCooling holder cryogen: NITROGEN
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: OTHER / Details: ab initio
Final reconstructionAlgorithm: FOURIER SPACE / Resolution.type: BY AUTHOR / Resolution: 1.8 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 2056878
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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