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Yorodumi- EMDB-39556: Cryo-EM structure of the Helicobacter pylori OorDABC complex in t... -
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Open data
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Basic information
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| Title | Cryo-EM structure of the Helicobacter pylori OorDABC complex in the apo-form | ||||||||||||||||||||||||
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Sample |
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Keywords | Oxoglutarate Oxidoreductase / Electron Transport / Tricarboxylic Acid Cycle / OXIDOREDUCTASE | ||||||||||||||||||||||||
| Function / homology | Function and homology information2-oxoglutarate synthase activity / small molecule metabolic process / thiamine pyrophosphate binding Similarity search - Function | ||||||||||||||||||||||||
| Biological species | ![]() | ||||||||||||||||||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 2.95 Å | ||||||||||||||||||||||||
Authors | Lan W / Gao Y / Bi H | ||||||||||||||||||||||||
| Funding support | China, 7 items
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Citation | Journal: To Be PublishedTitle: Cryo-EM structure of the Helicobacter pylori OorDABC complex in the apo-form Authors: Lan W / Gao Y / Bi H | ||||||||||||||||||||||||
| History |
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Structure visualization
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_39556.map.gz | 117.9 MB | EMDB map data format | |
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| Header (meta data) | emd-39556-v30.xml emd-39556.xml | 20 KB 20 KB | Display Display | EMDB header |
| Images | emd_39556.png | 26.7 KB | ||
| Filedesc metadata | emd-39556.cif.gz | 7 KB | ||
| Others | emd_39556_half_map_1.map.gz emd_39556_half_map_2.map.gz | 116.2 MB 116.2 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-39556 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-39556 | HTTPS FTP |
-Validation report
| Summary document | emd_39556_validation.pdf.gz | 845.4 KB | Display | EMDB validaton report |
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| Full document | emd_39556_full_validation.pdf.gz | 845 KB | Display | |
| Data in XML | emd_39556_validation.xml.gz | 14 KB | Display | |
| Data in CIF | emd_39556_validation.cif.gz | 16.6 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-39556 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-39556 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 8ys5MC M: atomic model generated by this map C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_39556.map.gz / Format: CCP4 / Size: 125 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 0.82 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: #2
| File | emd_39556_half_map_1.map | ||||||||||||
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| Density Histograms |
-Half map: #1
| File | emd_39556_half_map_2.map | ||||||||||||
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| Projections & Slices |
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| Density Histograms |
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Sample components
-Entire : Helicobacter pylori OorDABC complex in the apo-form
| Entire | Name: Helicobacter pylori OorDABC complex in the apo-form |
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| Components |
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-Supramolecule #1: Helicobacter pylori OorDABC complex in the apo-form
| Supramolecule | Name: Helicobacter pylori OorDABC complex in the apo-form / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#4 |
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| Source (natural) | Organism: ![]() |
-Macromolecule #1: 2-oxoglutarate:acceptor oxidoreductase
| Macromolecule | Name: 2-oxoglutarate:acceptor oxidoreductase / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 12.467625 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MAKMSTPDGV AVWVNEDRCK GCDICVSVCP AGVLGMGIEK ERVLGKVAKV AYPESCIGCV QCELHCPDFA IYVADRKDFK FAKVSKEAQ ERSEKVKANK YMLLEETILE GRGK UniProtKB: UNIPROTKB: A0A0B2EGL0 |
-Macromolecule #2: 2-oxoglutarate synthase subunit alpha
| Macromolecule | Name: 2-oxoglutarate synthase subunit alpha / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 41.565902 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MREIISDGNE LVAKAAIEVG CRFFGGYPIT PSSDIMHAMS VALPKCGGHF IQMEDEISGI SVSLGASMSG TKSMTASSGP GISLKVEQI GYSFMAEIPL VIADVMRSGP STGMPTRVAQ GDVNFLKHPI HGDFKAVALA PASLEEAYTE TVRAFNLAEM L MTPVFLLM ...String: MREIISDGNE LVAKAAIEVG CRFFGGYPIT PSSDIMHAMS VALPKCGGHF IQMEDEISGI SVSLGASMSG TKSMTASSGP GISLKVEQI GYSFMAEIPL VIADVMRSGP STGMPTRVAQ GDVNFLKHPI HGDFKAVALA PASLEEAYTE TVRAFNLAEM L MTPVFLLM DETVGHMYGK VQIPDLEEVQ KMTINRKEFV GDKKDYKPYG VAQDEPAVLN PFFKGYRYHV SGLHHGPIGF PT EDAKIGG DLIDRLFHKI ESKQDIINEN EEMDLEGAEI VIIAYGSVSL AVKEALKDYH KESKQKVGFF RPKTLWPSPA KRL KEIGDK YEKILVIELN KGQYLEEIER AMQRKVHFFG QANGRTISPK QIIAKLKEL UniProtKB: UNIPROTKB: A0A2T6W5S4 |
-Macromolecule #3: 2-oxoglutarate ferredoxin oxidoreductase subunit beta
| Macromolecule | Name: 2-oxoglutarate ferredoxin oxidoreductase subunit beta / type: protein_or_peptide / ID: 3 / Number of copies: 2 / Enantiomer: LEVO / EC number: 2-oxoglutarate synthase |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 30.481701 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MAFNYDEYLR VDKIPTLWCW GCGDGVILKS IIRTIDALGW KMDDVCLVSG IGCSGRMSSY VNCNTVHTTH GRAVAYATGI KMANPSKHV IVVSGDGDGF AIGGNHTMHA CRRNIDLNFI LVNNFIYGLT NSQTSPTTPN GMWTVTAQWG NIDNQFDPCA L TTAAGASF ...String: MAFNYDEYLR VDKIPTLWCW GCGDGVILKS IIRTIDALGW KMDDVCLVSG IGCSGRMSSY VNCNTVHTTH GRAVAYATGI KMANPSKHV IVVSGDGDGF AIGGNHTMHA CRRNIDLNFI LVNNFIYGLT NSQTSPTTPN GMWTVTAQWG NIDNQFDPCA L TTAAGASF VARESVLDPQ KLEKVLKEGF SHKGFSFFDV HSNCHINLGR KNKMGEASQM LKWMESRLVS KRQFEAMSPE ER VDKFPTG VLRHDTDRKE YCEAYQEIIE KAQGKQ UniProtKB: 2-oxoglutarate ferredoxin oxidoreductase subunit beta |
-Macromolecule #4: 2-oxoglutarate:acceptor oxidoreductase
| Macromolecule | Name: 2-oxoglutarate:acceptor oxidoreductase / type: protein_or_peptide / ID: 4 / Number of copies: 2 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 20.253453 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MEAQLRFTGV GGQGVLLAGE ILAEAKIVSG GYGTKTSTYT SQVRGGPTKV DILLDKDEII FPYAKEGEID FMLSVAQISY NQFKSDIKQ GGIVVIDPNL VTPTKEDEEK YQIYKIPIIS IAKDEVGNII TQSVVALAIT VELTKCVEEN IVLDTMLKKV P AKVADTNK KAFEIGKKHA LEALKVRA UniProtKB: UNIPROTKB: A0A0B2EEZ8 |
-Macromolecule #5: IRON/SULFUR CLUSTER
| Macromolecule | Name: IRON/SULFUR CLUSTER / type: ligand / ID: 5 / Number of copies: 6 / Formula: SF4 |
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| Molecular weight | Theoretical: 351.64 Da |
| Chemical component information | ![]() ChemComp-FS1: |
-Macromolecule #6: MAGNESIUM ION
| Macromolecule | Name: MAGNESIUM ION / type: ligand / ID: 6 / Number of copies: 2 / Formula: MG |
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| Molecular weight | Theoretical: 24.305 Da |
-Macromolecule #7: THIAMINE DIPHOSPHATE
| Macromolecule | Name: THIAMINE DIPHOSPHATE / type: ligand / ID: 7 / Number of copies: 2 / Formula: TPP |
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| Molecular weight | Theoretical: 425.314 Da |
| Chemical component information | ![]() ChemComp-TPP: |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Buffer | pH: 8 |
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| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 60.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.8 µm / Nominal defocus min: 1.2 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Keywords
Authors
China, 7 items
Citation



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Processing
FIELD EMISSION GUN
