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Yorodumi- PDB-9ku3: Cryo-EM structure of CtpA S300A/K325A/Q329A mutant from Helicobac... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 9ku3 | |||||||||||||||||||||
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| Title | Cryo-EM structure of CtpA S300A/K325A/Q329A mutant from Helicobacter pylori | |||||||||||||||||||||
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Keywords | HYDROLASE / Carboxyl-terminal processing protease / CtpA | |||||||||||||||||||||
| Function / homology | Function and homology informationserine-type peptidase activity / outer membrane-bounded periplasmic space / endopeptidase activity / signal transduction / proteolysis Similarity search - Function | |||||||||||||||||||||
| Biological species | Helicobacter pylori G27 (bacteria)![]() | |||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.14 Å | |||||||||||||||||||||
Authors | Sun, K. / Zhang, H. / Au, S.W.N. | |||||||||||||||||||||
| Funding support | Hong Kong, 1items
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Citation | Journal: To Be PublishedTitle: Cryo-EM structure of CtpA S300A/K325A/Q329A mutant from Helicobacter pylori Authors: Sun, K. / Zhang, H. / Au, S.W.N. | |||||||||||||||||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 9ku3.cif.gz | 433.1 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb9ku3.ent.gz | 357.4 KB | Display | PDB format |
| PDBx/mmJSON format | 9ku3.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 9ku3_validation.pdf.gz | 1.4 MB | Display | wwPDB validaton report |
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| Full document | 9ku3_full_validation.pdf.gz | 1.4 MB | Display | |
| Data in XML | 9ku3_validation.xml.gz | 62.1 KB | Display | |
| Data in CIF | 9ku3_validation.cif.gz | 99.5 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ku/9ku3 ftp://data.pdbj.org/pub/pdb/validation_reports/ku/9ku3 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 62573MC 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 |
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Links
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Assembly
| Deposited unit | ![]()
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Components
| #1: Protein | Mass: 45987.055 Da / Num. of mol.: 6 / Mutation: S300A, K325A, Q329A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Helicobacter pylori G27 (bacteria) / Strain: G27 / Gene: HPG27_1298 / Production host: ![]() #2: RNA chain | Mass: 635.881 Da / Num. of mol.: 6 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Has protein modification | N | |
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-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
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| EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
| Component | Name: Carboxyl-terminal processing protease CtpA S300A/K325A/Q329A mutant from Helicobacter pylori Type: COMPLEX / Entity ID: all / Source: MULTIPLE SOURCES |
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| Molecular weight | Value: 0.28 MDa / Experimental value: YES |
| Source (natural) | Organism: Helicobacter pylori G27 (bacteria) |
| Source (recombinant) | Organism: ![]() |
| Buffer solution | pH: 7.5 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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| 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: 2500 nm / Nominal defocus min: 1500 nm |
| Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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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: 3.14 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 151917 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refinement | Highest resolution: 3.14 Å Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS) | ||||||||||||||||||||||||
| Refine LS restraints |
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Helicobacter pylori G27 (bacteria)
Hong Kong, 1items
Citation
PDBj

FIELD EMISSION GUN