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- EMDB-47346: Cryo-EM structure of a TatBC complex from Nitratifractor salsuginis -
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Open data
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Basic information
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Title | Cryo-EM structure of a TatBC complex from Nitratifractor salsuginis | ||||||||||||
![]() | deepemhanced map used for model refinement | ||||||||||||
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![]() | Membrane Protein / TatC / TatB / twin-arginine translocation / TRANSLOCASE | ||||||||||||
Function / homology | ![]() proton motive force dependent protein transmembrane transporter activity / TAT protein transport complex / protein transport by the Tat complex / intracellular protein transmembrane transport / protein transmembrane transporter activity Similarity search - Function | ||||||||||||
Biological species | ![]() | ||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.5 Å | ||||||||||||
![]() | Deme JC / Bryant OJ / Berks BC / Lea SM | ||||||||||||
Funding support | ![]() ![]()
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![]() | ![]() Title: Structure of the twin-arginine protein translocation pathway core complex and the molecular basis for substrate recognition Authors: Deme JC / Bryant OJ / Berks BC / Lea SM | ||||||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 182.3 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 23.8 KB 23.8 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 14.3 KB | Display | ![]() |
Images | ![]() | 163 KB | ||
Masks | ![]() | 216 MB | ![]() | |
Filedesc metadata | ![]() | 6 KB | ||
Others | ![]() ![]() ![]() ![]() ![]() | 106.5 MB 1.2 MB 203.7 MB 200.7 MB 200.7 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 730.3 KB | Display | ![]() |
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Full document | ![]() | 729.9 KB | Display | |
Data in XML | ![]() | 21.5 KB | Display | |
Data in CIF | ![]() | 27.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9e02MC ![]() 9dzzC ![]() 9e01C ![]() 9e03C ![]() 9e04C ![]() 9e06C ![]() 9e07C ![]() 9e08C ![]() 9e0sC M: atomic model generated by this map 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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Map
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Annotation | deepemhanced map used for model refinement | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.723 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Mask #1
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Projections & Slices |
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Density Histograms |
-Additional map: unsharpened map
File | emd_47346_additional_1.map | ||||||||||||
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Annotation | unsharpened map | ||||||||||||
Projections & Slices |
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Density Histograms |
-Additional map: mask used for FSC calculation
File | emd_47346_additional_2.map | ||||||||||||
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Annotation | mask used for FSC calculation | ||||||||||||
Projections & Slices |
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Density Histograms |
-Additional map: B-factor sharpened map
File | emd_47346_additional_3.map | ||||||||||||
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Annotation | B-factor sharpened map | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: half map 2
File | emd_47346_half_map_1.map | ||||||||||||
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Annotation | half map 2 | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: half map 1
File | emd_47346_half_map_2.map | ||||||||||||
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Annotation | half map 1 | ||||||||||||
Projections & Slices |
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Density Histograms |
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Sample components
-Entire : TatBC complex
Entire | Name: TatBC complex |
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Components |
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-Supramolecule #1: TatBC complex
Supramolecule | Name: TatBC complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() |
-Macromolecule #1: Sec-independent protein translocase protein TatC
Macromolecule | Name: Sec-independent protein translocase protein TatC / type: protein_or_peptide / ID: 1 / Number of copies: 3 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 42.954797 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MFESMKPHLA ELRQRLAISV LAVFVGFIIA FTFHNAILGW ITKPLNNALI QVGKIVEKRE MGTWKISGNE HNATLAPSKS PALLSDHAQ SAEKLHRTLA EASQATQNPK LQKLLSQAAS AAEELARNSR ILRKALVKEE NLTRQAVNQN LREKSFNGMI T THQVGGAF ...String: MFESMKPHLA ELRQRLAISV LAVFVGFIIA FTFHNAILGW ITKPLNNALI QVGKIVEKRE MGTWKISGNE HNATLAPSKS PALLSDHAQ SAEKLHRTLA EASQATQNPK LQKLLSQAAS AAEELARNSR ILRKALVKEE NLTRQAVNQN LREKSFNGMI T THQVGGAF FVALKVSFFA GILMAMPVIL WQLWLFIAPG LYDNEKKMVL PFVVGGSVMF LIGVLFAYYV VTPFGFQFLI TF GSFLYTP LINIEDYVGF FTKILIGFGI AFELPVVAYF LALLGLITDK TLKDYFKYAI VIIFLLAAFL TPPDVLTQLL MAA PLILLY GLSILIVHYV NPYKPEEKED DEEEEEDEFE KAEREFEALE KGSESHESGS ENLYFQ UniProtKB: Sec-independent protein translocase protein TatC |
-Macromolecule #2: Sec-independent protein translocase protein TatB homolog
Macromolecule | Name: Sec-independent protein translocase protein TatB homolog type: protein_or_peptide / ID: 2 / Number of copies: 3 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 21.44168 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MFGMGFSEIL VIALVAILFL GPDKLPEAMV QIAKFFNSVR KTINEAKSTF EEELHLKELK EEALSYRQSL SEVGSDISGF KNAISNHTD ELQEAIEIAR SGMPTDRLNE SVDDLLEEDE PTGETSQRPG VTEYKEMARK ALEEAENSAE AQTAETPSVE D KGPESSPK ...String: MFGMGFSEIL VIALVAILFL GPDKLPEAMV QIAKFFNSVR KTINEAKSTF EEELHLKELK EEALSYRQSL SEVGSDISGF KNAISNHTD ELQEAIEIAR SGMPTDRLNE SVDDLLEEDE PTGETSQRPG VTEYKEMARK ALEEAENSAE AQTAETPSVE D KGPESSPK ESSRPAGFKH LDNEANAWSH PQFEK UniProtKB: Sec-independent protein translocase protein TatB homolog |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.4 |
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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: FEI FALCON IV (4k x 4k) / Average electron dose: 54.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 0.5 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |