+ Open data
Open data
- Basic information
Basic information
| Entry | Database: PDB / ID: 9kyc | ||||||
|---|---|---|---|---|---|---|---|
| Title | PltBd1/PltBd2 heteropentameric holotoxin from E. coli | ||||||
|  Components | 
 | ||||||
|  Keywords | TOXIN / heteropentamer | ||||||
| Function / homology |  Function and homology information catalytic activity / NAD+ poly-ADP-ribosyltransferase activity / extracellular region Similarity search - Function | ||||||
| Biological species |  Salmonella enterica subsp. diarizonae (bacteria) | ||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.94 Å | ||||||
|  Authors | Chen, Z. / Wang, D.D. / Gao, X. | ||||||
| Funding support | 1items 
 | ||||||
|  Citation |  Journal: To Be Published Title: Functional Synergy of Heteropentameric B Subunits Underlies Virulence in a Salmonella A2B5 Toxin Authors: Wang, D. / Chen, Z. / Xu, C. / Jiao, X. / Yue, M. / Gao, X. | ||||||
| History | 
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- Structure visualization
Structure visualization
| Structure viewer | Molecule:  Molmil  Jmol/JSmol | 
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- Downloads & links
Downloads & links
- Download
Download
| PDBx/mmCIF format |  9kyc.cif.gz | 218.3 KB | Display |  PDBx/mmCIF format | 
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| PDB format |  pdb9kyc.ent.gz | Display |  PDB format | |
| PDBx/mmJSON format |  9kyc.json.gz | Tree view |  PDBx/mmJSON format | |
| Others |  Other downloads | 
-Validation report
| Summary document |  9kyc_validation.pdf.gz | 1.5 MB | Display |  wwPDB validaton report | 
|---|---|---|---|---|
| Full document |  9kyc_full_validation.pdf.gz | 1.5 MB | Display | |
| Data in XML |  9kyc_validation.xml.gz | 39.7 KB | Display | |
| Data in CIF |  9kyc_validation.cif.gz | 59.6 KB | Display | |
| Arichive directory |  https://data.pdbj.org/pub/pdb/validation_reports/ky/9kyc  ftp://data.pdbj.org/pub/pdb/validation_reports/ky/9kyc | HTTPS FTP | 
-Related structure data
| Related structure data |  62644MC  9kybC  9kydC  9kyeC M: map data used to model this data C: citing same article ( | 
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| Similar structure data | Similarity search - Function & homology  F&H Search | 
- Links
Links
- Assembly
Assembly
| Deposited unit |  
 | 
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| 1 | 
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- Components
Components
| #1: Protein | Mass: 30184.424 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.)  Salmonella enterica subsp. diarizonae (bacteria) Gene: B4V94_22780, CTQ69_05285, DLB95_17835, G0D72_21670, GB480_00980, GBX62_11500 Production host:   Escherichia coli (E. coli) / References: UniProt: A0A3V0PQJ3 | ||||
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| #2: Protein | Mass: 27297.820 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.)  Salmonella enterica subsp. diarizonae (bacteria) Gene: artA, ABB53_009925, B4V94_22795, CNQ75_07295, DLB95_17850, G2916_21300, G2974_22565, G2997_22660, G3A00_19430, GB016_19575, GB034_20690, GB088_22285, GB236_21915, GB246_19590, GB337_19740, ...Gene: artA, ABB53_009925, B4V94_22795, CNQ75_07295, DLB95_17850, G2916_21300, G2974_22565, G2997_22660, G3A00_19430, GB016_19575, GB034_20690, GB088_22285, GB236_21915, GB246_19590, GB337_19740, GB348_18480, GB480_00965, GBS30_22125, GBV97_20145, GBW00_19900, GBX19_22040, GBX62_11515, GBY11_22700, GBY15_15100, GBY49_11210, GBZ04_18540, GBZ10_19960, GBZ12_10540, GBZ37_18520, GBZ41_22405 Production host:   Escherichia coli (E. coli) / References: UniProt: A0A2I5HFM6 | ||||
| #3: Protein | Mass: 16576.629 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.)  Salmonella enterica subsp. diarizonae (bacteria) Gene: DLB95_17855, G0D47_10640, G2916_21295, G2997_22655, G3A00_19435, GB016_19580, GB034_20695, GB088_22290, GB236_21910, GB246_19595, GB337_19745, GB348_18485, GBS30_22120, GBV97_20140, GBW00_ ...Gene: DLB95_17855, G0D47_10640, G2916_21295, G2997_22655, G3A00_19435, GB016_19580, GB034_20695, GB088_22290, GB236_21910, GB246_19595, GB337_19745, GB348_18485, GBS30_22120, GBV97_20140, GBW00_19905, GBX19_22045, GBX62_11520, GBY11_22705, GBY15_15095, GBY49_11215, GBZ10_19965, GBZ12_10545, GBZ37_18525, GBZ41_22400, PG27_18440 Production host:   Escherichia coli (E. coli) / References: UniProt: A0A3Z3F2I6 #4: Protein | Mass: 12920.474 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.)  Salmonella enterica subsp. diarizonae (bacteria) Gene: AH359_15415, B4V94_22805, CNQ75_07285, CTQ69_05310, FNI27_02145, G0D47_10645, G2974_22970, GBZ04_18550, JMJ85_10105, PG27_18445 Production host:   Escherichia coli (E. coli) / References: UniProt: A0A2I5HFM4 Has protein modification | Y |  | 
-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY | 
|---|---|
| EM experiment | Aggregation state: 3D ARRAY / 3D reconstruction method: single particle reconstruction | 
- Sample preparation
Sample preparation
| Component | Name: Recombinant Diarizonae toxin (DT) heteropentamer - PltA and PltBd1/Bd2 complex Type: COMPLEX / Entity ID: all / Source: RECOMBINANT | 
|---|---|
| Source (natural) | Organism:  Salmonella enterica subsp. diarizonae (bacteria) | 
| Source (recombinant) | Organism:   Escherichia coli (E. coli) | 
| Buffer solution | pH: 7.8 | 
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | 
| Vitrification | Cryogen name: ETHANE | 
- Electron microscopy imaging
Electron microscopy imaging
| Experimental equipment |  Model: Titan Krios / Image courtesy: FEI Company | 
|---|---|
| Microscopy | Model: TFS KRIOS | 
| Electron gun | Electron source:  FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM | 
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2000 nm / Nominal defocus min: 500 nm | 
| Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) | 
- Processing
Processing
| EM software | Name: PHENIX / Version: 1.20.1_4487 / Category: model refinement | ||||||||||||||||||||||||
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 2.94 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 144112 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refinement | Highest resolution: 2.94 Å Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS) | ||||||||||||||||||||||||
| Refine LS restraints | 
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