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- EMDB-44419: Structure of Clostridioides difficile Component A (50-463) in Com... -
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Open data
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Basic information
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Title | Structure of Clostridioides difficile Component A (50-463) in Complex with a CDTb Oligomer | |||||||||
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![]() | Clostridioides / difficile / toxin / CDT / TRANSFERASE | |||||||||
Function / homology | ![]() Transferases; Glycosyltransferases; Pentosyltransferases / protein homooligomerization / transferase activity / nucleotide binding / extracellular region / metal ion binding / identical protein binding Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.6 Å | |||||||||
![]() | Sheedlo MJ / Mullard RM | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Structure of Clostridioides difficile Component A (50-463) in Complex with a CDTb Oligomer Authors: Sheedlo MJ / Mullard RM | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 141.3 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 18.8 KB 18.8 KB | Display Display | ![]() |
Images | ![]() | 36.7 KB | ||
Filedesc metadata | ![]() | 6.5 KB | ||
Others | ![]() ![]() | 139 MB 139 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9bbfMC 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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Related items in Molecule of the Month |
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Map
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.65 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #2
File | emd_44419_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_44419_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
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Sample components
-Entire : Clostridioides difficile Transferase component A in complex with ...
Entire | Name: Clostridioides difficile Transferase component A in complex with Clostridioides difficile Transferase component B |
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Components |
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-Supramolecule #1: Clostridioides difficile Transferase component A in complex with ...
Supramolecule | Name: Clostridioides difficile Transferase component A in complex with Clostridioides difficile Transferase component B type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2 |
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Source (natural) | Organism: ![]() |
-Macromolecule #1: ADP-ribosyltransferase binding component
Macromolecule | Name: ADP-ribosyltransferase binding component / type: protein_or_peptide / ID: 1 / Number of copies: 7 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 94.289367 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MEIVNEDILP NNGLMGYYFT DEHFKDLKLM APIKDGNLKF EEKKVDKLLD KDKSDVKSIR WTGRIIPSKD GEYTLSTDRD DVLMQVNTE STISNTLKVN MKKGKEYKVR IELQDKNLGS IDNLSSPNLY WELDGMKKII PEENLFLRDY SNIEKDDPFI P NNNFFDPK ...String: MEIVNEDILP NNGLMGYYFT DEHFKDLKLM APIKDGNLKF EEKKVDKLLD KDKSDVKSIR WTGRIIPSKD GEYTLSTDRD DVLMQVNTE STISNTLKVN MKKGKEYKVR IELQDKNLGS IDNLSSPNLY WELDGMKKII PEENLFLRDY SNIEKDDPFI P NNNFFDPK LMSDWEDEDL DTDNDNIPDS YERNGYTIKD LIAVKWEDSF AEQGYKKYVS NYLESNTAGD PYTDYEKASG SF DKAIKTE ARDPLVAAYP IVGVGMEKLI ISTNEHASTD QGKTVSRATT NSKTESNTAG VSVNVGYQNG FTANVTTNYS HTT DNSTAV QDSNGESWNT GLSINKGESA YINANVRYYN TGTAPMYKVT PTTNLVLDGD TLSTIKAQEN QIGNNLSPGD TYPK KGLSP LALNTMDQFS SRLIPINYDQ LKKLDAGKQI KLETTQVSGN FGTKNSSGQI VTEGNSWSDY ISQIDSISAS IILDT ENES YERRVTAKNL QDPEDKTPEL TIGEAIEKAF GATKKDGLLY FNDIPIDESC VELIFDDNTA NKIKDSLKTL SDKKIY NVK LERGMNILIK TPTYFTNFDD YNNYPSTWSN VNTTNQDGLQ GSANKLNGET KIKIPMSELK PYKRYVFSGY SKDPLTS NS IIVKIKAKEE KTDYLVPEQG YTKFSYEFET TEKDSSNIEI TLIGSGTTYL DNLSITELNS TPEILDEPEV KIPTDQEI M DAHKIYFADL NFNPSTGNTY INGMYFAPTQ TNKEALDYIQ KYRVEATLQY SGFKDIGTKD KEMRNYLGDP NQPKTNYVN LRSYFTGGEN IMTYKKLRIY AITPDDRELL VLSVD UniProtKB: ADP-ribosyltransferase binding component |
-Macromolecule #2: ADP-ribosyltransferase enzymatic component
Macromolecule | Name: ADP-ribosyltransferase enzymatic component / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 47.626613 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: KAPIERPEDF LKDKEKAKEW ERKEAERIEQ KLERSEKEAL ESYKKDSVEI SKYSQTRNYF YDYQIEANSR EKEYKELRNA ISKNKIDKP MYVYYFESPE KFAFNKVIRT ENQNEISLEK FNEFKETIQN KLFKQDGFKD ISLYEPGKGD EKPTPLLMHL K LPRNTGML ...String: KAPIERPEDF LKDKEKAKEW ERKEAERIEQ KLERSEKEAL ESYKKDSVEI SKYSQTRNYF YDYQIEANSR EKEYKELRNA ISKNKIDKP MYVYYFESPE KFAFNKVIRT ENQNEISLEK FNEFKETIQN KLFKQDGFKD ISLYEPGKGD EKPTPLLMHL K LPRNTGML PYTNTNNVST LIEQGYSIKI DKIVRIVIDG KHYIKAEASV VSSLDFKDDV SKGDSWGKAN YNDWSNKLTP NE LADVNDY MRGGYTAINN YLISNGPVNN PNPELDSKIT NIENALKREP IPTNLTVYRR SGPQEFGLTL TSPEYDFNKL ENI DAFKSK WEGQALSYPN FISTSIGSVN MSAFAKRKIV LRITIPKGSP GAYLSAIPGY AGEYEVLLNH GSKFKINKID SYKD GTITK LIVDATLIP UniProtKB: ADP-ribosyltransferase enzymatic component |
-Macromolecule #3: CALCIUM ION
Macromolecule | Name: CALCIUM ION / type: ligand / ID: 3 / Number of copies: 14 / Formula: CA |
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Molecular weight | Theoretical: 40.078 Da |
-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: 8 |
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Grid | Model: Quantifoil R2/1 / Material: COPPER / Mesh: 200 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 45 sec. |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 295 K / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 52.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 0.5 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |