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- EMDB-34664: Cryo-EM structure of the Mycobacterium tuberculosis cytochrome bc... -

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Basic information

Entry
Database: EMDB / ID: EMD-34664
TitleCryo-EM structure of the Mycobacterium tuberculosis cytochrome bcc:aa3 supercomplex and a novel inhibitor targeting subunit cytochrome cI
Map data
Sample
  • Complex: Cytochrome bcc:aa3 supercomplex
    • Protein or peptide: x 9 types
  • Ligand: x 4 types
KeywordsCytochrome bcc:aa3 oxidase / Mycobacterium tuberculosis / OXIDOREDUCTASE
Function / homology
Function and homology information


oxidoreduction-driven active transmembrane transporter activity / aerobic electron transport chain / cytochrome-c oxidase / oxidative phosphorylation / quinol-cytochrome-c reductase / oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen / ubiquinol-cytochrome-c reductase activity / cytochrome-c oxidase activity / : / electron transport coupled proton transport ...oxidoreduction-driven active transmembrane transporter activity / aerobic electron transport chain / cytochrome-c oxidase / oxidative phosphorylation / quinol-cytochrome-c reductase / oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen / ubiquinol-cytochrome-c reductase activity / cytochrome-c oxidase activity / : / electron transport coupled proton transport / monooxygenase activity / aerobic respiration / respiratory electron transport chain / 2 iron, 2 sulfur cluster binding / electron transfer activity / iron ion binding / heme binding / membrane / metal ion binding / plasma membrane
Similarity search - Function
Protein of unknown function DUF5130 / Domain of unknown function (DUF5130) / Cytochrome bc1 complex, cytochrome c subunit / Cytochrome c oxidase subunit IV, actinobacteria / QcrA subunit, N-terminal / Cytochrome c oxidase subunit IV / QcrA subunit N-terminal region / Cytochrome b(N-terminal)/b6/petB / Cytochrome c oxidase, subunit I bacterial type / Cytochrome C oxidase, cbb3-type, subunit III ...Protein of unknown function DUF5130 / Domain of unknown function (DUF5130) / Cytochrome bc1 complex, cytochrome c subunit / Cytochrome c oxidase subunit IV, actinobacteria / QcrA subunit, N-terminal / Cytochrome c oxidase subunit IV / QcrA subunit N-terminal region / Cytochrome b(N-terminal)/b6/petB / Cytochrome c oxidase, subunit I bacterial type / Cytochrome C oxidase, cbb3-type, subunit III / Cytochrome c oxidase subunit III / Cytochrome c oxidase subunit III-like / Cytochrome c oxidase, subunit III, 4-helical bundle / Cytochrome c oxidase subunit III / Heme-copper oxidase subunit III family profile. / Cytochrome c oxidase subunit III-like superfamily / Cytochrome c oxidase, subunit I, copper-binding site / Heme-copper oxidase catalytic subunit, copper B binding region signature. / Cytochrome c oxidase-like, subunit I domain / Cytochrome oxidase subunit I profile. / Cytochrome c oxidase subunit I / Cytochrome c oxidase-like, subunit I superfamily / Cytochrome C and Quinol oxidase polypeptide I / 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 / Cytochrome c / Rieske [2Fe-2S] iron-sulphur domain / Rieske [2Fe-2S] 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
Cytochrome bc1 complex Rieske iron-sulfur subunit / Cytochrome c oxidase polypeptide 4 / Cytochrome bc1 complex cytochrome b subunit / DUF5130 domain-containing protein / Cytochrome bc1 complex cytochrome c subunit / Probable cytochrome c oxidase subunit 3 / Probable cytochrome c oxidase subunit 1
Similarity search - Component
Biological speciesMycobacterium tuberculosis variant bovis BCG (bacteria)
Methodelectron tomography / cryo EM
AuthorsMathiyazakan V / Gruber G
Funding support Singapore, 1 items
OrganizationGrant numberCountry
National Research Foundation (NRF, Singapore)NRF-CRP18-2017-01 Singapore
CitationJournal: Antimicrob Agents Chemother / Year: 2023
Title: Cryo-Electron Microscopy Structure of the s Cytochrome : Supercomplex and a Novel Inhibitor Targeting Subunit Cytochrome I.
Authors: Vikneswaran Mathiyazakan / Chui-Fann Wong / Amaravadhi Harikishore / Kevin Pethe / Gerhard Grüber /
Abstract: The mycobacterial cytochrome complex deserves the name "supercomplex" since it combines three cytochrome oxidases-cytochrome , cytochrome , and cytochrome -into one supramolecular machine and ...The mycobacterial cytochrome complex deserves the name "supercomplex" since it combines three cytochrome oxidases-cytochrome , cytochrome , and cytochrome -into one supramolecular machine and performs electron transfer for the reduction of oxygen to water and proton transport to generate the proton motive force for ATP synthesis. Thus, the complex represents a valid drug target for Mycobacterium tuberculosis infections. The production and purification of an entire M. tuberculosis cytochrome are fundamental for biochemical and structural characterization of this supercomplex, paving the way for new inhibitor targets and molecules. Here, we produced and purified the entire and active M. tuberculosis cyt- oxidase, as demonstrated by the different heme spectra and an oxygen consumption assay. The resolved M. tuberculosis cyt- cryo-electron microscopy structure reveals a dimer with its functional domains involved in electron, proton, oxygen transfer, and oxygen reduction. The structure shows the two cytochrome III head domains of the dimer, the counterpart of the soluble mitochondrial cytochrome , in a so-called "closed state," in which electrons are translocated from the to the domain. The structural and mechanistic insights provided the basis for a virtual screening campaign that identified a potent M. tuberculosis cyt- inhibitor, cyt1. cyt1 targets the mycobacterium-specific α3-helix of cytochrome I and interferes with oxygen consumption by interrupting electron translocation via the III head. The successful identification of a new cyt- inhibitor demonstrates the potential of a structure-mechanism-based approach for novel compound development.
History
DepositionNov 2, 2022-
Header (metadata) releaseMay 3, 2023-
Map releaseMay 3, 2023-
UpdateSep 13, 2023-
Current statusSep 13, 2023Processing site: PDBj / Status: Released

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Structure visualization

Supplemental images

emd_34664.png

Downloads & links

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Map

FileDownload / File: emd_34664.map.gz / Format: CCP4 / Size: 476.8 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Voxel sizeX=Y=Z: 1.06 Å
Density
Minimum - Maximum-0.6385015 - 1.9265063
Average (Standard dev.)0.0024210492 (±0.034254897)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions500500500
Spacing500500500
CellA=B=C: 530.0 Å
α=β=γ: 90.0 °

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Supplemental data

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Sample components

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Entire : Cytochrome bcc:aa3 supercomplex

EntireName: Cytochrome bcc:aa3 supercomplex
Components
  • Complex: Cytochrome bcc:aa3 supercomplex
    • Protein or peptide: Cytochrome bc1 complex Rieske iron-sulfur subunit
    • Protein or peptide: Cytochrome bc1 complex cytochrome b subunit
    • Protein or peptide: Cytochrome bc1 complex cytochrome c subunit
    • Protein or peptide: CYTOCHROME AA3 SUBUNIT CtaC
    • Protein or peptide: Probable cytochrome c oxidase subunit 1
    • Protein or peptide: Probable cytochrome c oxidase subunit 3
    • Protein or peptide: Cytochrome c oxidase polypeptide 4
    • Protein or peptide: CYTOCHROME AA3 SUBUNIT CtaJ
    • Protein or peptide: DUF5130 domain-containing protein
  • Ligand: FE2/S2 (INORGANIC) CLUSTER
  • Ligand: PROTOPORPHYRIN IX CONTAINING FE
  • Ligand: HEME C
  • Ligand: HEME-A

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Supramolecule #1: Cytochrome bcc:aa3 supercomplex

SupramoleculeName: Cytochrome bcc:aa3 supercomplex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#9
Source (natural)Organism: Mycobacterium tuberculosis variant bovis BCG (bacteria)

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Macromolecule #1: Cytochrome bc1 complex Rieske iron-sulfur subunit

MacromoleculeName: Cytochrome bc1 complex Rieske iron-sulfur subunit / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Mycobacterium tuberculosis variant bovis BCG (bacteria)
Molecular weightTheoretical: 46.976465 KDa
Recombinant expressionOrganism: Mycobacterium tuberculosis variant bovis BCG (bacteria)
SequenceString: MSRADDDAVG VPPTCGGRSD EEERRIVPGP NPQDGAKDGA KATAVPREPD EAALAAMSNQ ELLALGGKLD GVRIAYKEPR WPVEGTKAE KRAERSVAVW LLLGGVFGLA LLLIFLFWPW EFKAADGESD FIYSLTTPLY GLTFGLSILS IAIGAVLYQK R FIPEEISI ...String:
MSRADDDAVG VPPTCGGRSD EEERRIVPGP NPQDGAKDGA KATAVPREPD EAALAAMSNQ ELLALGGKLD GVRIAYKEPR WPVEGTKAE KRAERSVAVW LLLGGVFGLA LLLIFLFWPW EFKAADGESD FIYSLTTPLY GLTFGLSILS IAIGAVLYQK R FIPEEISI QERHDGASRE IDRKTVVANL TDAFEGSTIR RRKLIGLSFG VGMGAFGLGT LVAFAGGLIK NPWKPVVPTA EG KKAVLWT SGWTPRYQGE TIYLARATGT EDGPPFIKMR PEDMDAGGME TVFPWRESDG DGTTVESHHK LQEIAMGIRN PVM LIRIKP SDLGRVVKRK GQESFNFGEF FAFTKVCSHL GCPSSLYEQQ SYRILCPCHQ SQFDALHFAK PIFGPAARAL AQLP ITIDT DGYLVANGDF VEPVGPAFWE RTTT

UniProtKB: Cytochrome bc1 complex Rieske iron-sulfur subunit

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Macromolecule #2: Cytochrome bc1 complex cytochrome b subunit

MacromoleculeName: Cytochrome bc1 complex cytochrome b subunit / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO / EC number: quinol-cytochrome-c reductase
Source (natural)Organism: Mycobacterium tuberculosis variant bovis BCG (bacteria)
Molecular weightTheoretical: 63.925984 KDa
Recombinant expressionOrganism: Mycobacterium tuberculosis variant bovis BCG (bacteria)
SequenceString: MSPKLSPPNI GEVLARQAED IDTRYHPSAA LRRQLNKVFP THWSFLLGEI ALYSFVVLLI TGVYLTLFFD PSMVDVTYNG VYQPLRGVE MSRAYQSALD ISFEVRGGLF VRQIHHWAAL MFAAAIMVHL ARIFFTGAFR RPRETNWVIG SLLLILAMFE G YFGYSLPD ...String:
MSPKLSPPNI GEVLARQAED IDTRYHPSAA LRRQLNKVFP THWSFLLGEI ALYSFVVLLI TGVYLTLFFD PSMVDVTYNG VYQPLRGVE MSRAYQSALD ISFEVRGGLF VRQIHHWAAL MFAAAIMVHL ARIFFTGAFR RPRETNWVIG SLLLILAMFE G YFGYSLPD DLLSGLGLRA ALSSITLGMP VIGTWLHWAL FGGDFPGTIL IPRLYALHIL LLPGIILALI GLHLALVWFQ KH TQFPGPG RTEHNVVGVR VMPVFAFKSG AFFAAIVGVL GLMGGLLQIN PIWNLGPYKP SQVSAGSQPD FYMMWTEGLA RIW PPWEFY FWHHTIPAPV WVAVIMGLVF VLLPAYPFLE KRFTGDYAHH NLLQRPRDVP VRTAIGAMAI AFYMVLTLAA MNDI IALKF HISLNATTWI GRIGMVILPP FVYFITYRWC IGLQRSDRSV LEHGVETGII KRLPHGAYIE LHQPLGPVDE HGHPI PLQY QGAPLPKRMN KLGSAGSPGS GSFLFADSAA EDAALREAGH AAEQRALAAL REHQDSIMGS PDGEHGGGGE NLYFQD YKD DDDKHHHHHH

UniProtKB: Cytochrome bc1 complex cytochrome b subunit

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Macromolecule #3: Cytochrome bc1 complex cytochrome c subunit

MacromoleculeName: Cytochrome bc1 complex cytochrome c subunit / type: protein_or_peptide / ID: 3 / Number of copies: 2 / Enantiomer: LEVO / EC number: quinol-cytochrome-c reductase
Source (natural)Organism: Mycobacterium tuberculosis variant bovis BCG (bacteria)
Molecular weightTheoretical: 29.170404 KDa
Recombinant expressionOrganism: Mycobacterium tuberculosis variant bovis BCG (bacteria)
SequenceString: MTKLGFTRSG GSKSGRTRRR LRRRLSGGVL LLIALTIAGG LAAVLTPTPQ VAVADESSSA LLRTGKQLFD TSCVSCHGAN LQGVPDHGP SLIGVGEAAV YFQVSTGRMP AMRGEAQAPR KDPIFDEAQI DAIGAYVQAN GGGPTVVRNP DGSIATQSLR G NDLGRGGD ...String:
MTKLGFTRSG GSKSGRTRRR LRRRLSGGVL LLIALTIAGG LAAVLTPTPQ VAVADESSSA LLRTGKQLFD TSCVSCHGAN LQGVPDHGP SLIGVGEAAV YFQVSTGRMP AMRGEAQAPR KDPIFDEAQI DAIGAYVQAN GGGPTVVRNP DGSIATQSLR G NDLGRGGD LFRLNCASCH NFTGKGGALS SGKYAPDLAP ANEQQILTAM LTGPQNMPKF SNRQLSFEAK KDIIAYVKVA TE ARQPGGY LLGGFGPAPE GMAMWIIGMV AAIGLALWIG ARS

UniProtKB: Cytochrome bc1 complex cytochrome c subunit

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Macromolecule #4: CYTOCHROME AA3 SUBUNIT CtaC

MacromoleculeName: CYTOCHROME AA3 SUBUNIT CtaC / type: protein_or_peptide / ID: 4 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Mycobacterium tuberculosis variant bovis BCG (bacteria)
Molecular weightTheoretical: 40.535582 KDa
Recombinant expressionOrganism: Mycobacterium tuberculosis variant bovis BCG (bacteria)
SequenceString: MTPRGPGRLQ RLSQCRPQRG SGGPARGLRQ LALAAMLGAL AVTVSGCSWS EALGIGWPEG ITPEAHLNRE LWIGAVIASL AVGVIVWGL IFWSAVFHRK KNTDTELPRQ FGYNMPLELV LTVIPFLIIS VLFYFTVVVQ EKMLQIAKDP EVVIDITSFQ W NWKFGYQR ...String:
MTPRGPGRLQ RLSQCRPQRG SGGPARGLRQ LALAAMLGAL AVTVSGCSWS EALGIGWPEG ITPEAHLNRE LWIGAVIASL AVGVIVWGL IFWSAVFHRK KNTDTELPRQ FGYNMPLELV LTVIPFLIIS VLFYFTVVVQ EKMLQIAKDP EVVIDITSFQ W NWKFGYQR VNFKDGTLTY DGADPERKRA MVSKPEGKDK YGEELVGPVR GLNTEDRTYL NFDKVETLGT STEIPVLVLP SG KRIEFQM ASADVIHAFW VPEFLFKRDV MPNPVANNSV NVFQIEEIIK TGAFVGHCAE MCGTYHSMMN FEVRVVTPND FKA YLQQRI DGKTNAEALR AINQPPLAVT THPFDTRRGE LAPQPVG

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Macromolecule #5: Probable cytochrome c oxidase subunit 1

MacromoleculeName: Probable cytochrome c oxidase subunit 1 / type: protein_or_peptide / ID: 5 / Number of copies: 2 / Enantiomer: LEVO / EC number: cytochrome-c oxidase
Source (natural)Organism: Mycobacterium tuberculosis variant bovis BCG (bacteria)
Molecular weightTheoretical: 63.722289 KDa
Recombinant expressionOrganism: Mycobacterium tuberculosis variant bovis BCG (bacteria)
SequenceString: MTAEAPPLGE LEAIRPYPAR TGPKGSLVYK LITTTDHKMI GIMYCVACIS FFFIGGLLAL LMRTELAAPG LQFLSNEQFN QLFTMHGTI MLLFYATPIV FGFANLVLPL QIGAPDVAFP RLNAFSFWLF VFGATIGAAG FITPGGAADF GWTAYTPLTD A IHSPGAGG ...String:
MTAEAPPLGE LEAIRPYPAR TGPKGSLVYK LITTTDHKMI GIMYCVACIS FFFIGGLLAL LMRTELAAPG LQFLSNEQFN QLFTMHGTI MLLFYATPIV FGFANLVLPL QIGAPDVAFP RLNAFSFWLF VFGATIGAAG FITPGGAADF GWTAYTPLTD A IHSPGAGG DLWIMGLIVA GLGTILGAVN MITTVVCMRA PGMTMFRMPI FTWNIMVTSI LILIAFPLLT AALFGLAADR HL GAHIYDA ANGGVLLWQH LFWFFGHPEV YIIALPFFGI VSEIFPVFSR KPIFGYTTLV YATLSIAALS VAVWAHHMFA TGA VLLPFF SFMTYLIAVP TGIKFFNWIG TMWKGQLTFE TPMLFSVGFM VTFLLGGLTG VLLASPPLDF HVTDSYFVVA HFHY VLFGT IVFATFAGIY FWFPKMTGRL LDERLGKLHF WLTFIGFHTT FLVQHWLGDE GMPRRYADYL PTDGFQGLNV VSTIG AFIL GASMFPFVWN VFKSWRYGEV VTVDDPWGYG NSLEWATSCP PPRHNFTELP RIRSERPAFE LHYPHMVERL RAEAHV GRH HDEPAMVTSS

UniProtKB: Probable cytochrome c oxidase subunit 1

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Macromolecule #6: Probable cytochrome c oxidase subunit 3

MacromoleculeName: Probable cytochrome c oxidase subunit 3 / type: protein_or_peptide / ID: 6 / Number of copies: 2 / Enantiomer: LEVO / EC number: cytochrome-c oxidase
Source (natural)Organism: Mycobacterium tuberculosis variant bovis BCG (bacteria)
Molecular weightTheoretical: 22.435021 KDa
Recombinant expressionOrganism: Mycobacterium tuberculosis variant bovis BCG (bacteria)
SequenceString: MTSAVGTSGT AITSRVHSLN RPNMVSVGTI VWLSSELMFF AGLFAFYFSA RAQAGGNWPP PPTELNLYQA VPVTLVLIAS SFTCQMGVF AAERGDIFGL RRWYVITFLM GLFFVLGQAY EYRNLMSHGT SIPSSAYGSV FYLATGFHGL HVTGGLIAFI F LLVRTGMS ...String:
MTSAVGTSGT AITSRVHSLN RPNMVSVGTI VWLSSELMFF AGLFAFYFSA RAQAGGNWPP PPTELNLYQA VPVTLVLIAS SFTCQMGVF AAERGDIFGL RRWYVITFLM GLFFVLGQAY EYRNLMSHGT SIPSSAYGSV FYLATGFHGL HVTGGLIAFI F LLVRTGMS KFTPAQATAS IVVSYYWHFV DIVWIALFTV IYFIR

UniProtKB: Probable cytochrome c oxidase subunit 3

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Macromolecule #7: Cytochrome c oxidase polypeptide 4

MacromoleculeName: Cytochrome c oxidase polypeptide 4 / type: protein_or_peptide / ID: 7 / Number of copies: 2 / Enantiomer: LEVO / EC number: cytochrome-c oxidase
Source (natural)Organism: Mycobacterium tuberculosis variant bovis BCG (bacteria)
Molecular weightTheoretical: 14.874137 KDa
Recombinant expressionOrganism: Mycobacterium tuberculosis variant bovis BCG (bacteria)
SequenceString:
MHIEARLFEF VAAFFVVTAV LYGVLTSMFA TGGVEWAGTT ALALTGGMAL IVATFFRFVA RRLDSRPEDY EGAEISDGAG ELGFFSPHS WWPIMVALSG SVAAVGIALW LPWLIAAGVA FILASAAGLV FEYYVGPEKH

UniProtKB: Cytochrome c oxidase polypeptide 4

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Macromolecule #8: CYTOCHROME AA3 SUBUNIT CtaJ

MacromoleculeName: CYTOCHROME AA3 SUBUNIT CtaJ / type: protein_or_peptide / ID: 8 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Mycobacterium tuberculosis variant bovis BCG (bacteria)
Molecular weightTheoretical: 8.408646 KDa
Recombinant expressionOrganism: Mycobacterium tuberculosis variant bovis BCG (bacteria)
SequenceString:
MSAMEIHLFF VGIPLLLVVV LSVLIWSRKG PHPATYKLSE PWTHPPILWA ATDVVGSAHG GHGHDASEFT VGGGASGTW

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Macromolecule #9: DUF5130 domain-containing protein

MacromoleculeName: DUF5130 domain-containing protein / type: protein_or_peptide / ID: 9 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Mycobacterium tuberculosis variant bovis BCG (bacteria)
Molecular weightTheoretical: 15.982042 KDa
Recombinant expressionOrganism: Mycobacterium tuberculosis variant bovis BCG (bacteria)
SequenceString:
MARGDVATIE HAELPPGWVL TTSGRISGVT EPGELSVHYP FPIADLVALD DALTYSSRAC QVRFAIYLGD LGRDTAARAR EILGKVPTP DNAVLLAVSP NQCAIEVVYG SQVRGRGAES AAPLGVAAAS SAFEQGELVD GLISAIRVLS AGIAPG

UniProtKB: DUF5130 domain-containing protein

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Macromolecule #10: FE2/S2 (INORGANIC) CLUSTER

MacromoleculeName: FE2/S2 (INORGANIC) CLUSTER / type: ligand / ID: 10 / Number of copies: 2 / Formula: FES
Molecular weightTheoretical: 175.82 Da
Chemical component information

ChemComp-FES:
FE2/S2 (INORGANIC) CLUSTER

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Macromolecule #11: PROTOPORPHYRIN IX CONTAINING FE

MacromoleculeName: PROTOPORPHYRIN IX CONTAINING FE / type: ligand / ID: 11 / 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 #12: HEME C

MacromoleculeName: HEME C / type: ligand / ID: 12 / Number of copies: 4 / Formula: HEC
Molecular weightTheoretical: 618.503 Da
Chemical component information

ChemComp-HEC:
HEME C

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Macromolecule #13: HEME-A

MacromoleculeName: HEME-A / type: ligand / ID: 13 / Number of copies: 4 / Formula: HEA
Molecular weightTheoretical: 852.837 Da
Chemical component information

ChemComp-HEA:
HEME-A

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Experimental details

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Structure determination

Methodcryo EM
Processingelectron tomography
Aggregation stateparticle

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Sample preparation

BufferpH: 7.4
VitrificationCryogen name: ETHANE
SectioningOther: NO SECTIONING

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: SUPER-RESOLUTION / Average electron dose: 40.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.0 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Final reconstructionNumber images used: 100

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