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Yorodumi- EMDB-51692: The Cryo-EM structure of bacterial beta-1,3-glucan phosphorylase ... -
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Open data
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Basic information
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| Title | The Cryo-EM structure of bacterial beta-1,3-glucan phosphorylase from family GH161 | |||||||||
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Keywords | Glycoside phosphorylase / GH161 / beta-1 / 3-glucan phosphorylase / SUGAR BINDING PROTEIN | |||||||||
| Biological species | Bacteria (eubacteria) / unclassified Bacteria (bacteria) | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 2.32 Å | |||||||||
Authors | Cioci G / Cooper N / Ladeveze S / Shayan R | |||||||||
| Funding support | France, 1 items
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Citation | Journal: To Be PublishedTitle: The Cryo-EM structure of bacterial beta-1,3-glucan phosphorylase from family GH161 Authors: Cioci G / Cooper N / Ladeveze S / Shayan R | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_51692.map.gz | 78.9 MB | EMDB map data format | |
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| Header (meta data) | emd-51692-v30.xml emd-51692.xml | 18.6 KB 18.6 KB | Display Display | EMDB header |
| Images | emd_51692.png | 21.7 KB | ||
| Filedesc metadata | emd-51692.cif.gz | 6.6 KB | ||
| Others | emd_51692_half_map_1.map.gz emd_51692_half_map_2.map.gz | 79.2 MB 79.2 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-51692 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-51692 | HTTPS FTP |
-Validation report
| Summary document | emd_51692_validation.pdf.gz | 815.5 KB | Display | EMDB validaton report |
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| Full document | emd_51692_full_validation.pdf.gz | 815.1 KB | Display | |
| Data in XML | emd_51692_validation.xml.gz | 13.3 KB | Display | |
| Data in CIF | emd_51692_validation.cif.gz | 15.8 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-51692 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-51692 | HTTPS FTP |
-Related structure data
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Map
| File | Download / File: emd_51692.map.gz / Format: CCP4 / Size: 103 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: 0.822 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: #2
| File | emd_51692_half_map_1.map | ||||||||||||
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| Density Histograms |
-Half map: #1
| File | emd_51692_half_map_2.map | ||||||||||||
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| Density Histograms |
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Sample components
-Entire : GH161_MS (metanode satellite) Homodimeric enzyme
| Entire | Name: GH161_MS (metanode satellite) Homodimeric enzyme |
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| Components |
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-Supramolecule #1: GH161_MS (metanode satellite) Homodimeric enzyme
| Supramolecule | Name: GH161_MS (metanode satellite) Homodimeric enzyme / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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| Source (natural) | Organism: Bacteria (eubacteria) |
-Macromolecule #1: beta-1,3-glucan phosphorylase
| Macromolecule | Name: beta-1,3-glucan phosphorylase / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO |
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| Source (natural) | Organism: unclassified Bacteria (bacteria) |
| Molecular weight | Theoretical: 118.987039 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: ETFVMDDYGK KSTFASFLPG IAGIRGIPIW CYYVNRGQCV VSFGVDNKDH AIMEFYPAHQ AYQNVKTTGF RTFLKKNGTV FEPFSDENI THRMQIHMNG LAIEEQNRSS GMDTKVVYYT LPGENVGALV RVVSVTNQSG EPIELELIDG MPAVIPYGVS M DSMKNMGQ ...String: ETFVMDDYGK KSTFASFLPG IAGIRGIPIW CYYVNRGQCV VSFGVDNKDH AIMEFYPAHQ AYQNVKTTGF RTFLKKNGTV FEPFSDENI THRMQIHMNG LAIEEQNRSS GMDTKVVYYT LPGENVGALV RVVSVTNQSG EPIELELIDG MPAVIPYGVS M DSMKNMGQ TAKAWMQVED LSEGLPYYRV RASMDDTAAV RRIDGGNFSA CCEADGRRLQ PIVDPSLIFS YDLSLKRPVG FE ERPLKEL LLEEQMTQNL LPCSFYGITR TLAPGGSVTL YELIGQVENK QLLKEYFAEK KDAAYFEAKK READELAEAL TDG IRTRTA SAAFDAYCRY TYMDNVLRGG YPMQLGNNKI FYVYSRKHGD LERDYNYFSM LPEFYSQGNG NFRDVNQNRR CDTF FAPFV GRKNIQEFYS LIQLDGYNPL GVEKLTYRLS KERAKKLLTD VKEEQRSALI DFATKPFTPG ALCRKFGEVF GDTWD ETLF IRVIDFAEEM VNGSFGEGYW SDHWTYNLDL ILDYLSVFPE QEKEMLYEEV YTTFLSRINV NRRFRRYVET ENGLRQ YRA LNEASRRAAA AEKLVRTEYG SGDVLTMTLM EKLILLGAVK FATLDAYGMG IEMEGGKPGW YDALNGMPGL FGSSMAE TY ELARMLSYTI EALKQYPGEV ALIEELGCFL DELNLITRLE HDNIMRDEEL LSFWNRINDA KEIYRDKTYQ GVSGKKMV Y HTEQLAAILE GFLEIVTCGI KKARRISGEI CPTYFTYEVP EYEKLKDGGI RPLKFVPQNM PYFLEGPVRY LKLPVEQGE KRALYEAVKE SDLYDGELSM YKVNASLADS SFELGRARAF TPGWLENESI WLHMEYKYLL ELLRSGLYEE FFADFKKAAI PFQNPEIYG RSIYENSSFI ASSRNPNPSC RGRGFVARLS GSTIEFISMW KEMMFGAHPF RTEQEELVFS LAPAIPAYLI P EDGRLSAA FMSKTTVCYE FGGHRDYVPG TYRIRHMVFF YENGSQATVE GEKVSGKLAE DIRAGRVRKM EVAVDLEHHH H |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Concentration | 1 mg/mL | |||||||||
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| Buffer | pH: 7.4 Component:
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| Grid | Model: UltrAuFoil R1.2/1.3 / Material: GOLD / Mesh: 300 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 45 sec. / Details: 12 mA | |||||||||
| Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK I |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Image recording | Film or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 38.38 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: 3.0 µm / Nominal defocus min: 0.9 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
-Atomic model buiding 1
| Initial model | Chain - Source name: AlphaFold / Chain - Initial model type: in silico model |
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| Refinement | Space: REAL / Protocol: FLEXIBLE FIT / Target criteria: Cross-correlation coeficient |
| Output model | ![]() PDB-9gy9: |
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About Yorodumi



Keywords
unclassified Bacteria (bacteria)
Authors
France, 1 items
Citation


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FIELD EMISSION GUN
