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Open data
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Basic information
Entry | ![]() | |||||||||
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Title | State 1 Hdr-focused map Elp-Hdr | |||||||||
![]() | Hdr focused map of the conformational state 1 of the Elp-Hdr complex | |||||||||
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![]() | Redox / Flavin-based electron bifurcation / methanogenesis / heterodisulfide reductase / F420-H2 oxidase / Oxidoreductase | |||||||||
Function / homology | ![]() H2:CoB-CoM heterodisulfide,ferredoxin reductase / CoB--CoM heterodisulfide reductase activity / methanogenesis / 4 iron, 4 sulfur cluster binding / metal ion binding / membrane / plasma membrane Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.2 Å | |||||||||
![]() | San Segundo-Acosta P / Murphy BJ | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Altered electron flow in hydrogenotrophic methanogens under nickel limitation Authors: Nomura S / San Segundo-Acosta P / Kahnt J / Murphy BJ / Shima S | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 301.8 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 22.3 KB 22.3 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 14.7 KB | Display | ![]() |
Images | ![]() | 55.7 KB | ||
Filedesc metadata | ![]() | 6.1 KB | ||
Others | ![]() ![]() | 318.1 MB 318.1 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8rvuC ![]() 8rvvC ![]() 8rvyC ![]() 8rwnC C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
File | ![]() | ||||||||||||||||||||||||||||||||||||
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Annotation | Hdr focused map of the conformational state 1 of the Elp-Hdr complex | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.837 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: Half A of the Hdr focused map of...
File | emd_19535_half_map_1.map | ||||||||||||
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Annotation | Half A of the Hdr focused map of the conformational state 1 of the Elp-Hdr complex | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Half B of the Hdr focused map of...
File | emd_19535_half_map_2.map | ||||||||||||
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Annotation | Half B of the Hdr focused map of the conformational state 1 of the Elp-Hdr complex | ||||||||||||
Projections & Slices |
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Density Histograms |
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Sample components
-Entire : F420-dependent electron-donating proteins- heterodisulfide reduct...
Entire | Name: F420-dependent electron-donating proteins- heterodisulfide reductase complex (Elp-Hdr) from Methanothermobacter marburgensis (heterodisulfide reductase core and mobile arm, composite structure) |
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Components |
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-Supramolecule #1: F420-dependent electron-donating proteins- heterodisulfide reduct...
Supramolecule | Name: F420-dependent electron-donating proteins- heterodisulfide reductase complex (Elp-Hdr) from Methanothermobacter marburgensis (heterodisulfide reductase core and mobile arm, composite structure) type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 450 KDa |
-Macromolecule #1: CoB-CoM heterodisulfide,ferredoxin reductase subunit A
Macromolecule | Name: CoB-CoM heterodisulfide,ferredoxin reductase subunit A type: protein_or_peptide / ID: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Sequence | String: MAEEKKETME EPKIGVYVCH CGVNIGGVVD VEAVRDYAAK LPNVVIAKDY KYYCSDPGQL EIQKDIKELG INRVVVAACS PRLHEPTFRR CVEEAGLNQF LFEFANIREH DSWVHMDNPE GATEKAKDLV RMAVAKARLL EPLEASKVSV DDKALVIGGG VAGIQAALDL ...String: MAEEKKETME EPKIGVYVCH CGVNIGGVVD VEAVRDYAAK LPNVVIAKDY KYYCSDPGQL EIQKDIKELG INRVVVAACS PRLHEPTFRR CVEEAGLNQF LFEFANIREH DSWVHMDNPE GATEKAKDLV RMAVAKARLL EPLEASKVSV DDKALVIGGG VAGIQAALDL ADMGFKTYMV EKRPSISGRM GQLDKTFPTL DCSMCILAPK MVDVGKHDNI ELITYAEVKE VDGYIGNFKV KIEKKPRYID EELCTGCGSC VEVCPIEMPN YFDEGIGMTK AVYIPFPQAV PLCATIDKDY CIECMLCDEV CERGAVKHDQ EPEEIEIEVG TIIVATGYDA YDPTEKLEYG YGRHTNVITG LELERMINAS GPTDGKVLKP SDGEKPKRVA FIHCVGSRDE QIGKPYCSRV CCMYIMKNAQ LIKDKMPDTE VTLYYMDIRA FGKGFEEFYK RSQEKYGIKF IRGRPAEVIE NPDLTLTVRS EDTLLGKVTE YDYDMVVLGV GLVPPEGAET LRQTIGLSKS ADGFLMEAHP KLRPVDTLTD GVYLAGVAQG PKDIPDAVAQ ASGAAARAAI PMVKGEVEIE PIIAVTDSDV CGGCEVCIEL CPFGAISIEE GHANVNVALC KGCGTCVAAC PSGAMDQQHF KTEQIMAQIE AALNEPASK UniProtKB: H(2):CoB-CoM heterodisulfide,ferredoxin reductase subunit A |
-Macromolecule #2: CoB-CoM heterodisulfide,ferredoxin reductase subunit A
Macromolecule | Name: CoB-CoM heterodisulfide,ferredoxin reductase subunit A type: protein_or_peptide / ID: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Sequence | String: MAEEKKETME EPKIGVYVCH CGVNIGGVVD VEAVRDYAAK LPNVVIAKDY KYYCSDPGQL EIQKDIKELG INRVVVAACS PRLHEPTFRR CVEEAGLNQF LFEFANIREH DSWVHMDNPE GATEKAKDLV RMAVAKARLL EPLEASKVSV DDKALVIGGG VAGIQAALDL ...String: MAEEKKETME EPKIGVYVCH CGVNIGGVVD VEAVRDYAAK LPNVVIAKDY KYYCSDPGQL EIQKDIKELG INRVVVAACS PRLHEPTFRR CVEEAGLNQF LFEFANIREH DSWVHMDNPE GATEKAKDLV RMAVAKARLL EPLEASKVSV DDKALVIGGG VAGIQAALDL ADMGFKTYMV EKRPSISGRM GQLDKTFPTL DCSMCILAPK MVDVGKHDNI ELITYAEVKE VDGYIGNFKV KIEKKPRYID EELCTGCGSC VEVCPIEMPN YFDEGIGMTK AVYIPFPQAV PLCATIDKDY CIECMLCDEV CERGAVKHDQ EPEEIEIEVG TIIVATGYDA YDPTEKLEYG YGRHTNVITG LELERMINAS GPTDGKVLKP SDGEKPKRVA FIHCVGSRDE QIGKPYCSRV CCMYIMKNAQ LIKDKMPDTE VTLYYMDIRA FGKGFEEFYK RSQEKYGIKF IRGRPAEVIE NPDLTLTVRS EDTLLGKVTE YDYDMVVLGV GLVPPEGAET LRQTIGLSKS ADGFLMEAHP KLRPVDTLTD GVYLAGVAQG PKDIPDAVAQ ASGAAARAAI PMVKGEVEIE PIIAVTDSDV CGGCEVCIEL CPFGAISIEE GHANVNVALC KGCGTCVAAC PSGAMDQQHF KTEQIMAQIE AALNEPASK |
-Macromolecule #3: CoB-CoM heterodisulfide,ferredoxin reductase subunit B
Macromolecule | Name: CoB-CoM heterodisulfide,ferredoxin reductase subunit B type: protein_or_peptide / ID: 3 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Sequence | String: MEIAYFLGCI MNNRYPGIEK ATRVLFDKLG IELKDMEGAS CCPAPGVFGS FDKTTWAAIA ARNITIAEDM GADIMTECNG CFGSLFETN HLLKEDEEMK AKINEILKET GREYKGEVNV RHFAEVLYND VGLDKLSELV EKPLNLNVAV HYGCHFLKPS D EINIDNPE ...String: MEIAYFLGCI MNNRYPGIEK ATRVLFDKLG IELKDMEGAS CCPAPGVFGS FDKTTWAAIA ARNITIAEDM GADIMTECNG CFGSLFETN HLLKEDEEMK AKINEILKET GREYKGEVNV RHFAEVLYND VGLDKLSELV EKPLNLNVAV HYGCHFLKPS D EINIDNPE RPTILDEIVE VTGAKSVEYK DKMMCCGAGG GVRSRDLDVA LDFTREKLTN MKEAGVDAIV NVCPFCHLQF DV GQMEIKD KFGEEFDIPV LHLAQLLGLA MGLPKEDLVV DAHQVCVDEC LEKLEELDRL APGSG UniProtKB: H(2):CoB-CoM heterodisulfide,ferredoxin reductase subunit B |
-Macromolecule #4: CoB-CoM heterodisulfide,ferredoxin reductase subunit B
Macromolecule | Name: CoB-CoM heterodisulfide,ferredoxin reductase subunit B type: protein_or_peptide / ID: 4 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Sequence | String: MEIAYFLGCI MNNRYPGIEK ATRVLFDKLG IELKDMEGAS CCPAPGVFGS FDKTTWAAIA ARNITIAEDM GADIMTECNG CFGSLFETN HLLKEDEEMK AKINEILKET GREYKGEVNV RHFAEVLYND VGLDKLSELV EKPLNLNVAV HYGCHFLKPS D EINIDNPE ...String: MEIAYFLGCI MNNRYPGIEK ATRVLFDKLG IELKDMEGAS CCPAPGVFGS FDKTTWAAIA ARNITIAEDM GADIMTECNG CFGSLFETN HLLKEDEEMK AKINEILKET GREYKGEVNV RHFAEVLYND VGLDKLSELV EKPLNLNVAV HYGCHFLKPS D EINIDNPE RPTILDEIVE VTGAKSVEYK DKMMCCGAGG GVRSRDLDVA LDFTREKLTN MKEAGVDAIV NVCPFCHLQF DV GQMEIKD KFGEEFDIPV LHLAQLLGLA MGLPKEDLVV DAHQVCVDEC LEKLEELDRL APGSG |
-Macromolecule #5: CoB-CoM heterodisulfide,ferredoxin reductase subunit C
Macromolecule | Name: CoB-CoM heterodisulfide,ferredoxin reductase subunit C type: protein_or_peptide / ID: 5 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Sequence | String: MTLLQREENI IRKGNIDKEF SEKIKAAGGD SLEYCFQCGT CTGSCPSGRR TPYRVRQIIR KANVGLKDEI ISDPTLWMCT TCYSCQERC PRKVKIVDVV KLARNEAAKA GFMAPAHKAV GSFVIKTGHG VPINDATMEL RKAVGLGELP PTTHQFPEAL E EVQKIIKA TGFDQLIGYN WETGELE UniProtKB: H(2):CoB-CoM heterodisulfide,ferredoxin reductase subunit C |
-Macromolecule #6: CoB-CoM heterodisulfide,ferredoxin reductase subunit C
Macromolecule | Name: CoB-CoM heterodisulfide,ferredoxin reductase subunit C type: protein_or_peptide / ID: 6 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Sequence | String: MTLLQREENI IRKGNIDKEF SEKIKAAGGD SLEYCFQCGT CTGSCPSGRR TPYRVRQIIR KANVGLKDEI ISDPTLWMCT TCYSCQERC PRKVKIVDVV KLARNEAAKA GFMAPAHKAV GSFVIKTGHG VPINDATMEL RKAVGLGELP PTTHQFPEAL E EVQKIIKA TGFDQLIGYN WETGELE |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Concentration | 1 mg/mL |
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Buffer | pH: 7.6 Details: 50 mM Tris-HCl pH 7.6 containing 400 mM Ammonium sulfate. |
Vitrification | Cryogen name: NITROGEN / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Specialist optics | Energy filter - Name: GIF Bioquantum |
Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Number grids imaged: 1 / Number real images: 7768 / Average electron dose: 65.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.2 µm / Nominal defocus min: 0.8 µm |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
-Atomic model buiding 1
Initial model | Chain - Source name: Other / Chain - Initial model type: other / Details: Automated-based model building using Model-Angelo |
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Refinement | Space: REAL / Protocol: RIGID BODY FIT |