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Yorodumi- PDB-6ti2: Structure of the Ustilago maydis chorismate mutase 1 in complex w... -
+Open data
-Basic information
Entry | Database: PDB / ID: 6ti2 | ||||||
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Title | Structure of the Ustilago maydis chorismate mutase 1 in complex with KWL1-b from Zea mays | ||||||
Components |
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Keywords | CELL INVASION / kiwellin / chorismate mutase / smut / infection | ||||||
Function / homology | Function and homology information effector-mediated suppression of host salicylic acid-mediated innate immune signaling / host apoplast / chorismate metabolic process / chorismate mutase / chorismate mutase activity / host cell cytosol / aromatic amino acid family biosynthetic process / extracellular region Similarity search - Function | ||||||
Biological species | Ustilago maydis 521 (fungus) Zea mays (maize) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.75 Å | ||||||
Authors | Altegoer, F. / Bange, G. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2020 Title: The two paralogous kiwellin proteins KWL1 and KWL1-b from maize are structurally related and have overlapping functions in plant defense. Authors: Altegoer, F. / Weiland, P. / Giammarinaro, P.I. / Freibert, S.A. / Binnebesel, L. / Han, X. / Lepak, A. / Kahmann, R. / Lechner, M. / Bange, G. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6ti2.cif.gz | 214.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6ti2.ent.gz | 138.5 KB | Display | PDB format |
PDBx/mmJSON format | 6ti2.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ti/6ti2 ftp://data.pdbj.org/pub/pdb/validation_reports/ti/6ti2 | HTTPS FTP |
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-Related structure data
Related structure data | 6fpgS 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
#1: Protein | Mass: 31060.238 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Ustilago maydis 521 (fungus) / Gene: UMAG_05731 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: A0A0D1DWQ2, chorismate mutase #2: Protein | Mass: 21261.582 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Zea mays (maize) / Gene: 103642133, ZEAMMB73_Zm00001d026470 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: K7U7F7 #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.36 Å3/Da / Density % sol: 63.35 % |
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Crystal grow | Temperature: 294 K / Method: vapor diffusion, sitting drop / Details: 0.1 M HEPES pH 7.0, 8 % (w/v) PEG 8000 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID29 / Wavelength: 1.07252 Å |
Detector | Type: DECTRIS PILATUS3 S 6M / Detector: PIXEL / Date: Jun 28, 2018 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.07252 Å / Relative weight: 1 |
Reflection | Resolution: 2.75→48.82 Å / Num. obs: 35373 / % possible obs: 98.38 % / Redundancy: 3 % / Biso Wilson estimate: 74.77 Å2 / CC1/2: 0.992 / Rmerge(I) obs: 0.087 / Net I/σ(I): 8.31 |
Reflection shell | Resolution: 2.75→2.85 Å / Rmerge(I) obs: 0.705 / Mean I/σ(I) obs: 1.36 / Num. unique obs: 3546 / CC1/2: 0.615 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 6FPG Resolution: 2.75→47.99 Å / SU ML: 0.4873 / Cross valid method: FREE R-VALUE / σ(F): 1.37 / Phase error: 31.0755
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 73.82 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.75→47.99 Å
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Refine LS restraints |
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LS refinement shell |
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