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Yorodumi- PDB-3jc9: Architectural model of the type IVa pilus machine in a non-piliat... -
+Open data
-Basic information
Entry | Database: PDB / ID: 3jc9 | ||||||
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Title | Architectural model of the type IVa pilus machine in a non-piliated state | ||||||
Components |
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Keywords | MOTOR PROTEIN / motor / pilus / ring / membrane channel | ||||||
Function / homology | Function and homology information type IV pilus assembly / type IV pilus-dependent motility / protein secretion / cell outer membrane / cell division / membrane / plasma membrane Similarity search - Function | ||||||
Biological species | Myxococcus xanthus DK 1622 (bacteria) | ||||||
Method | ELECTRON MICROSCOPY / electron tomography / cryo EM | ||||||
Authors | Chang, Y.-W. / Rettberg, L.A. / Jensen, G.J. | ||||||
Citation | Journal: Science / Year: 2016 Title: Architecture of the type IVa pilus machine. Authors: Yi-Wei Chang / Lee A Rettberg / Anke Treuner-Lange / Janet Iwasa / Lotte Søgaard-Andersen / Grant J Jensen / Abstract: Type IVa pili are filamentous cell surface structures observed in many bacteria. They pull cells forward by extending, adhering to surfaces, and then retracting. We used cryo-electron tomography of ...Type IVa pili are filamentous cell surface structures observed in many bacteria. They pull cells forward by extending, adhering to surfaces, and then retracting. We used cryo-electron tomography of intact Myxococcus xanthus cells to visualize type IVa pili and the protein machine that assembles and retracts them (the type IVa pilus machine, or T4PM) in situ, in both the piliated and nonpiliated states, at a resolution of 3 to 4 nanometers. We found that T4PM comprises an outer membrane pore, four interconnected ring structures in the periplasm and cytoplasm, a cytoplasmic disc and dome, and a periplasmic stem. By systematically imaging mutants lacking defined T4PM proteins or with individual proteins fused to tags, we mapped the locations of all 10 T4PM core components and the minor pilins, thereby providing insights into pilus assembly, structure, and function. | ||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | Molecule: MolmilJmol/JSmol |
-Downloads & links
-Download
PDBx/mmCIF format | 3jc9.cif.gz | 2.4 MB | Display | PDBx/mmCIF format |
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PDB format | pdb3jc9.ent.gz | Display | PDB format | |
PDBx/mmJSON format | 3jc9.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 3jc9_validation.pdf.gz | 1.4 MB | Display | wwPDB validaton report |
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Full document | 3jc9_full_validation.pdf.gz | 1.5 MB | Display | |
Data in XML | 3jc9_validation.xml.gz | 330.9 KB | Display | |
Data in CIF | 3jc9_validation.cif.gz | 592.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/jc/3jc9 ftp://data.pdbj.org/pub/pdb/validation_reports/jc/3jc9 | HTTPS FTP |
-Related structure data
Related structure data | 3260MC 3247C 3248C 3249C 3250C 3251C 3252C 3253C 3254C 3255C 3256C 3257C 3258C 3259C 3261C 3262C 3263C 3264C 3jc8C M: map data used to model this data C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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-Components
-Protein , 8 types, 79 molecules AaAbAcAdAeCaCbNaNbNcNdNeNfNgNhNiNjNkNlOaObOcOdOeOfOgOhOiOjOk...
#1: Protein | Mass: 17210.494 Da / Num. of mol.: 5 / Source method: isolated from a natural source / Source: (natural) Myxococcus xanthus DK 1622 (bacteria) #2: Protein | Mass: 45191.023 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Myxococcus xanthus DK 1622 (bacteria) / References: UniProt: Q1D0A0 #3: Protein | Mass: 24889.914 Da / Num. of mol.: 12 / Source method: isolated from a natural source / Source: (natural) Myxococcus xanthus DK 1622 (bacteria) / References: UniProt: Q306N5 #4: Protein | Mass: 22911.150 Da / Num. of mol.: 12 / Source method: isolated from a natural source / Source: (natural) Myxococcus xanthus DK 1622 (bacteria) / References: UniProt: Q306N4 #5: Protein | Mass: 42267.102 Da / Num. of mol.: 12 / Source method: isolated from a natural source / Source: (natural) Myxococcus xanthus DK 1622 (bacteria) / References: UniProt: Q1D0B0 #6: Protein | Mass: 96199.984 Da / Num. of mol.: 12 / Source method: isolated from a natural source / Source: (natural) Myxococcus xanthus DK 1622 (bacteria) / References: UniProt: Q9ZFG1 #7: Protein | Mass: 18154.627 Da / Num. of mol.: 12 / Source method: isolated from a natural source / Source: (natural) Myxococcus xanthus DK 1622 (bacteria) / References: UniProt: Q306N3 #8: Protein | Mass: 44704.219 Da / Num. of mol.: 12 / Source method: isolated from a natural source / Source: (natural) Myxococcus xanthus DK 1622 (bacteria) / References: UniProt: Q1D813 |
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-Non-polymers , 2 types, 24 molecules
#9: Chemical | ChemComp-MG / #10: Chemical | ChemComp-ATP / |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: electron tomography |
-Sample preparation
Component | Name: Type IVa pilus machine in vivo / Type: COMPLEX |
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Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Instrument: FEI VITROBOT MARK III / Cryogen name: ETHANE Details: Plunged into liquid ethane (FEI VITROBOT MARK III). |
-Electron microscopy imaging
Experimental equipment | Model: Tecnai Polara / Image courtesy: FEI Company |
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Microscopy | Model: FEI POLARA 300 / Date: Dec 31, 2013 |
Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
Electron lens | Mode: BRIGHT FIELD / Nominal magnification: 27500 X / Cs: 2.2 mm |
Specimen holder | Temperature: 77 K / Tilt angle max: -60 ° / Tilt angle min: 60 ° |
Image recording | Electron dose: 150 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
EM imaging optics | Energyfilter upper: 20 eV / Energyfilter lower: 0 eV |
-Processing
EM software |
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Symmetry | Point symmetry: C2 (2 fold cyclic) | ||||||||||||
3D reconstruction | Method: Simultaneous iterative reconstruction technique / Nominal pixel size: 7.8 Å / Actual pixel size: 7.8 Å / Symmetry type: POINT | ||||||||||||
Refinement step | Cycle: LAST
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