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Yorodumi- PDB-5bw0: The crystal structure of minor pseudopilin binary complex of XcpV... -
+Open data
-Basic information
Entry | Database: PDB / ID: 5bw0 | ||||||
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Title | The crystal structure of minor pseudopilin binary complex of XcpV and XcpW from the Type 2 secretion system of Pseudomonas aeruginosa | ||||||
Components |
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Keywords | PROTEIN TRANSPORT | ||||||
Function / homology | Function and homology information protein secretion by the type II secretion system / type II protein secretion system complex / plasma membrane Similarity search - Function | ||||||
Biological species | Pseudomonas aeruginosa (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2 Å | ||||||
Authors | Zhang, Y. / Faucher, F. / Poole, K. / Jia, Z. | ||||||
Funding support | Canada, 1items
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Citation | Journal: PLoS Pathog. / Year: 2018 Title: Structure-guided disruption of the pseudopilus tip complex inhibits the Type II secretion in Pseudomonas aeruginosa. Authors: Zhang, Y. / Faucher, F. / Zhang, W. / Wang, S. / Neville, N. / Poole, K. / Zheng, J. / Jia, Z. #1: Journal: To Be Published Title: Inhibition of Pseudomonas aeruginosa Type II secretion by structure-based peptides Authors: Zhang, Y. / Faucher, F. / Poole, K. / Jia, Z. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5bw0.cif.gz | 222.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5bw0.ent.gz | 177.5 KB | Display | PDB format |
PDBx/mmJSON format | 5bw0.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/bw/5bw0 ftp://data.pdbj.org/pub/pdb/validation_reports/bw/5bw0 | HTTPS FTP |
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-Related structure data
Related structure data | 5vtmC 2retS S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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2 |
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3 |
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4 |
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Unit cell |
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-Components
#1: Protein | Mass: 20891.469 Da / Num. of mol.: 4 / Fragment: residues 28-204 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Pseudomonas aeruginosa (bacteria) / Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228 / Gene: xcpW, pddD, PA3098 / Production host: Escherichia coli (E. coli) / References: UniProt: Q00517 #2: Protein | Mass: 10736.025 Da / Num. of mol.: 4 / Fragment: residues 33-126 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Pseudomonas aeruginosa (bacteria) / Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228 / Gene: xcpV, pddC, PA3099 / Production host: Escherichia coli (E. coli) / References: UniProt: Q00516 #3: Chemical | ChemComp-SO4 / #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.29 Å3/Da / Density % sol: 46.39 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7 Details: 10-15% PEG 3350, 0.1M Tris, pH 7.0, 0.5M caesium chloride . Protein solution: 25mM HEPES, pH 7.0, 150mM sodium chloride |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 23-ID-B / Wavelength: 1.033 Å |
Detector | Type: MAR scanner 300 mm plate / Detector: IMAGE PLATE / Date: Aug 22, 2012 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.033 Å / Relative weight: 1 |
Reflection | Resolution: 2→19.7 Å / Num. obs: 68807 / % possible obs: 97.9 % / Redundancy: 8.7 % / Rmerge(I) obs: 0.11 / Net I/σ(I): 11.73 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 2RET Resolution: 2→19.7 Å / SU ML: 0.23 / Cross valid method: FREE R-VALUE / σ(F): 1.36 / Phase error: 28.74 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2→19.7 Å
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Refine LS restraints |
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LS refinement shell |
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