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Open data
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Basic information
| Entry | Database: PDB / ID: 9i3m | ||||||||||||||||||||||||||||||
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| Title | Csu pilus rod antiparallel pair | ||||||||||||||||||||||||||||||
Components | CsuA/B | ||||||||||||||||||||||||||||||
Keywords | CELL ADHESION / pili / fimbriae / Acinetobacter baumannii pili / chaperone-usher pathway / archaic chaperone-usher pili / biofilm / 3D biofilm / adhesion / pathogenesis / pilus antiparallel binding junction | ||||||||||||||||||||||||||||||
| Function / homology | : / Spore coat protein U / Spore Coat Protein U domain / Spore Coat Protein U domain / Spore coat protein U/FanG domain-containing protein Function and homology information | ||||||||||||||||||||||||||||||
| Biological species | Acinetobacter baumannii (bacteria) | ||||||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 8.91 Å | ||||||||||||||||||||||||||||||
Authors | Malmi, H. / Pakharukova, N. / Zavialov, A.V. | ||||||||||||||||||||||||||||||
| Funding support | Finland, 3items
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Citation | Journal: To Be PublishedTitle: Antiparallel stacking of Csu pili drives Acinetobacter baumannii 3D biofilm assembly Authors: Malmi, H. / Pakharukova, N. / Paul, B. / Tuittila, M. / Ahmad, I. / Knight, S.D. / Uhlin, B.E. / Ghosal, D. / Zavialov, A.V. | ||||||||||||||||||||||||||||||
| History |
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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 | 9i3m.cif.gz | 1.1 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9i3m.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9i3m.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/i3/9i3m ftp://data.pdbj.org/pub/pdb/validation_reports/i3/9i3m | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 52600MC ![]() 9i37C ![]() 9i3nC ![]() 9i3oC C: citing same article ( M: map data used to model this data |
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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: 16069.642 Da / Num. of mol.: 26 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Acinetobacter baumannii (bacteria) / Strain: 19096 / Gene: ATCC19606_12570 / Plasmid: pBAD-Csu / Cell (production host): Planktonic bacteria / Production host: ![]() Has protein modification | Y | |
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-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
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| EM experiment | Aggregation state: FILAMENT / 3D reconstruction method: single particle reconstruction |
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Sample preparation
| Component | Name: Csu pilus rod antiparallel pair / Type: COMPLEX Details: Csu pilus rods are homopolymers of subunit CsuA/B. The sample contains Csu pilus rods self-assembled into pairs through antiparallel interactions. Entity ID: all / Source: RECOMBINANT | |||||||||||||||
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| Molecular weight | Value: 16.05974 kDa/nm / Experimental value: NO | |||||||||||||||
| Source (natural) | Organism: Acinetobacter baumannii (bacteria) / Strain: 19096 / Cellular location: Outer membrane / Organelle: Outer membrane / Tissue: Planktonic bacteria | |||||||||||||||
| Source (recombinant) | Organism: ![]() | |||||||||||||||
| Buffer solution | pH: 7.4 Details: Sample is a fraction taken from an ion exchange column elution gradient, so the NaCl concentration may vary. | |||||||||||||||
| Buffer component |
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| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES Details: Csu pilus rods are homopolymers of subunit CsuA/B. The sample contains Csu pilus rods self-assembled into pairs through antiparallel interactions. The pairs and stacks accumulate over time ...Details: Csu pilus rods are homopolymers of subunit CsuA/B. The sample contains Csu pilus rods self-assembled into pairs through antiparallel interactions. The pairs and stacks accumulate over time in a sample tube containing purified Csu pili. | |||||||||||||||
| Specimen support | Grid material: COPPER / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil R1.2/1.3 | |||||||||||||||
| Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277.15 K |
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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 magnification: 105000 X / Nominal defocus max: 2500 nm / Nominal defocus min: 800 nm |
| Specimen holder | Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
| Image recording | Electron dose: 50 e/Å2 / Detector mode: SUPER-RESOLUTION / Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Num. of grids imaged: 1 |
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Processing
| EM software |
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Particle selection | Num. of particles selected: 35938 | ||||||||||||||||||||||||||||||||||||||||||||||||||
| 3D reconstruction | Resolution: 8.91 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 12883 / Symmetry type: POINT | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Atomic model building | B value: 304.76 / Protocol: RIGID BODY FIT / Space: REAL Details: UCSF Chimera was used to first fit the subunits into the single native pilus rod map (PDB Accession ID: 9I37) and average their relative angles, and it was also used to adjust pixel spacing ...Details: UCSF Chimera was used to first fit the subunits into the single native pilus rod map (PDB Accession ID: 9I37) and average their relative angles, and it was also used to adjust pixel spacing of all maps to match model dimensions. Coot was used to adjust side chain and loop positions. A pair of antiparallel pili with subunit angles adjusted to 3-turns-per-7-subunits symmetry was overlapped with a 2D class to adjust the binding junction angle. Finally, Phenix was used to fit the pair model into the map. | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Atomic model building | PDB-ID: 7ZL4 Accession code: 7ZL4 / Chain residue range: 24-178 Details: The initial model consisted of a single pilus rod fragment of the same type. The initial model in turn is based on a crystal structure of CsuA/Bsc with PDB accession code 6FM5. Pdb chain residue range: 24-178 / Source name: PDB / Type: experimental model |
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Acinetobacter baumannii (bacteria)
Finland, 3items
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