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Open data
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Basic information
Entry | Database: PDB / ID: 5b0o | ||||||
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Title | Structure of the FliH-FliI complex | ||||||
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![]() | HYDROLASE/MOTOR PROTEIN / Bacterial flagellum / type III secretion / ATPase / peripheral stalk / HYDROLASE-MOTOR PROTEIN complex | ||||||
Function / homology | ![]() bacterial-type flagellum organization / type III protein secretion system complex / bacterial-type flagellum / protein secretion by the type III secretion system / cytoskeletal motor activity / bacterial-type flagellum assembly / bacterial-type flagellum-dependent cell motility / proton-transporting ATP synthase complex, catalytic core F(1) / H+-transporting two-sector ATPase / proton-transporting ATPase activity, rotational mechanism ...bacterial-type flagellum organization / type III protein secretion system complex / bacterial-type flagellum / protein secretion by the type III secretion system / cytoskeletal motor activity / bacterial-type flagellum assembly / bacterial-type flagellum-dependent cell motility / proton-transporting ATP synthase complex, catalytic core F(1) / H+-transporting two-sector ATPase / proton-transporting ATPase activity, rotational mechanism / proton-transporting ATP synthase activity, rotational mechanism / protein transport / ATP hydrolysis activity / ATP binding / identical protein binding / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Imada, K. / Uchida, Y. / Kinoshita, M. / Namba, K. / Minamino, T. | ||||||
![]() | ![]() Title: Insight into the flagella type III export revealed by the complex structure of the type III ATPase and its regulator Authors: Imada, K. / Minamino, T. / Uchida, Y. / Kinoshita, M. / Namba, K. #1: Journal: Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. Year: 2012 Title: Crystallization and preliminary X-ray analysis of the FliH-FliI complex responsible for bacterial flagellar type III protein export. Authors: Uchida, Y. / Minamino, T. / Namba, K. / Imada, K. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 542.1 KB | Display | ![]() |
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PDB format | ![]() | 446.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.5 MB | Display | ![]() |
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Full document | ![]() | 1.6 MB | Display | |
Data in XML | ![]() | 108.2 KB | Display | |
Data in CIF | ![]() | 143.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2dpyS S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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4 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 49319.551 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: LT2 / SGSC1412 / ATCC 700720 / Gene: fliI, fla AIII, flaC, STM1972 / Plasmid: pET15b / Production host: Escherichia coli / Strain (production host): BL21(DE3) References: UniProt: P26465, H+-transporting two-sector ATPase #2: Protein | Mass: 15335.442 Da / Num. of mol.: 8 / Fragment: UNP residues 99-235 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #3: Chemical | ChemComp-ADP / |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.57 Å3/Da / Density % sol: 52.13 % |
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Crystal grow | Temperature: 285 K / Method: vapor diffusion, sitting drop / pH: 7.2 Details: 5%(w/v) PEG400, 0.1M HEPES pH7.2 and 100mM Magnesium acetate |
-Data collection
Diffraction | Mean temperature: 40 K / Ambient temp details: helium gas flow |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Feb 3, 2010 |
Radiation | Monochromator: Double-crystal monochromator / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 3→60 Å / Num. obs: 65054 / % possible obs: 99.4 % / Redundancy: 4.6 % / Rmerge(I) obs: 0.109 / Net I/σ(I): 9.4 |
Reflection shell | Resolution: 3→3.16 Å / Redundancy: 4.2 % / Rmerge(I) obs: 0.362 / Mean I/σ(I) obs: 3.5 / % possible all: 99.6 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 2DPY Resolution: 3→51.315 Å / SU ML: 0.96 / Cross valid method: THROUGHOUT / σ(F): 1.36 / Phase error: 25.8 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 1.06 Å / VDW probe radii: 1.3 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 37.271 Å2 / ksol: 0.267 e/Å3 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 3→51.315 Å
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Refine LS restraints |
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LS refinement shell |
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