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Yorodumi- PDB-4mn8: Crystal structure of flg22 in complex with the FLS2 and BAK1 ecto... -
+Open data
-Basic information
Entry | Database: PDB / ID: 4mn8 | |||||||||
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Title | Crystal structure of flg22 in complex with the FLS2 and BAK1 ectodomains | |||||||||
Components |
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Keywords | TRANSFERASE/TRANSFERASE RECEPTOR / FLS2 / BAK1 / flg22 / Flagellin / plant immunity / Leucine-rich repeat / TRANSFERASE-TRANSFERASE RECEPTOR complex | |||||||||
Function / homology | Function and homology information regulation of anion channel activity / defense response by callose deposition in cell wall / transmembrane receptor protein serine/threonine kinase activity / receptor serine/threonine kinase binding / endomembrane system / detection of bacterium / transmembrane receptor protein tyrosine kinase activity / phosphorylation / receptor-mediated endocytosis / receptor protein-tyrosine kinase ...regulation of anion channel activity / defense response by callose deposition in cell wall / transmembrane receptor protein serine/threonine kinase activity / receptor serine/threonine kinase binding / endomembrane system / detection of bacterium / transmembrane receptor protein tyrosine kinase activity / phosphorylation / receptor-mediated endocytosis / receptor protein-tyrosine kinase / defense response / non-specific serine/threonine protein kinase / endosome membrane / endosome / defense response to bacterium / protein serine kinase activity / signaling receptor binding / protein serine/threonine kinase activity / ATP binding / identical protein binding / membrane / plasma membrane Similarity search - Function | |||||||||
Biological species | Arabidopsis thaliana (thale cress) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.062 Å | |||||||||
Authors | Chai, J. / Sun, Y. / Han, Z. | |||||||||
Citation | Journal: Science / Year: 2013 Title: Structural basis for flg22-induced activation of the Arabidopsis FLS2-BAK1 immune complex. Authors: Sun, Y. / Li, L. / Macho, A.P. / Han, Z. / Hu, Z. / Zipfel, C. / Zhou, J.M. / Chai, J. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4mn8.cif.gz | 394.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4mn8.ent.gz | 323.1 KB | Display | PDB format |
PDBx/mmJSON format | 4mn8.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/mn/4mn8 ftp://data.pdbj.org/pub/pdb/validation_reports/mn/4mn8 | HTTPS FTP |
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-Related structure data
Related structure data | 4mnaC 3rgzS C: citing same article (ref.) S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
-Protein , 2 types, 2 molecules AB
#1: Protein | Mass: 85524.281 Da / Num. of mol.: 1 / Fragment: FLS2-LRR UNP RESIDUES 25-800 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Arabidopsis thaliana (thale cress) / Gene: FLS2, At5g46330, MPL12.13, MPL12.8 / Cell (production host): high five / Production host: Spodoptera frugiperda (fall armyworm) References: UniProt: Q9FL28, non-specific serine/threonine protein kinase |
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#2: Protein | Mass: 24631.170 Da / Num. of mol.: 1 / Fragment: BAK1-LRR UNP RESIDUES 1-220 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Arabidopsis thaliana (thale cress) / Gene: BAK1, ELG, SERK3, At4g33430, F17M5.190 / Cell (production host): high five / Production host: Spodoptera frugiperda (fall armyworm) References: UniProt: Q94F62, receptor protein-tyrosine kinase, non-specific serine/threonine protein kinase |
-Protein/peptide / Non-polymers , 2 types, 17 molecules C
#3: Protein/peptide | Mass: 2275.502 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: This sequence is synthetic produce |
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#6: Chemical | ChemComp-SO4 / |
-Sugars , 2 types, 10 molecules
#4: Polysaccharide | 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose Source method: isolated from a genetically manipulated source |
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#5: Sugar | ChemComp-NAG / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 4.52 Å3/Da / Density % sol: 72.81 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 4 Details: 0.1M citirc acid pH 4.0, 2.5M ammonium sulfate, 8% (v/v) PEG 400, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: SYNCHROTRON / Site: SSRF / Beamline: BL17U / Wavelength: 1 Å |
Detector | Type: ADSC QUANTUM 210 / Detector: CCD / Date: Jul 12, 2012 |
Radiation | Monochromator: SAGITALLY FOCUSED Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 3.05→50 Å / Num. all: 38964 / Num. obs: 38653 / % possible obs: 99.2 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 1 / Redundancy: 3.5 % |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 3RGZ Resolution: 3.062→29.962 Å / SU ML: 0.4 / σ(F): 0 / Phase error: 31.09 / 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: 3.062→29.962 Å
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Refine LS restraints |
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LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 14
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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