+Open data
-Basic information
Entry | Database: PDB / ID: 1ehc | ||||||
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Title | STRUCTURE OF SIGNAL TRANSDUCTION PROTEIN CHEY | ||||||
Components | CHEY | ||||||
Keywords | SIGNAL TRANSDUCTION / CHEY / RESPONSE REGULATORS / CHEMOTAXIS / SENSORY TRANSDUCTION / PHOSPHORYLATION / FLAGELLAR ROT | ||||||
Function / homology | Function and homology information bacterial-type flagellum basal body, C ring / bacterial-type flagellum rotor complex / bacterial-type flagellum-dependent swimming motility / regulation of bacterial-type flagellum-dependent cell motility / aerotaxis / bacterial-type flagellum / regulation of chemotaxis / thermotaxis / internal peptidyl-lysine acetylation / phosphorelay response regulator activity ...bacterial-type flagellum basal body, C ring / bacterial-type flagellum rotor complex / bacterial-type flagellum-dependent swimming motility / regulation of bacterial-type flagellum-dependent cell motility / aerotaxis / bacterial-type flagellum / regulation of chemotaxis / thermotaxis / internal peptidyl-lysine acetylation / phosphorelay response regulator activity / protein acetylation / acetyltransferase activity / phosphorelay signal transduction system / chemotaxis / magnesium ion binding / signal transduction / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / PHASED WITH WT / Resolution: 2.26 Å | ||||||
Authors | Jiang, M. / Bourret, R. / Simon, M. / Volz, K. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 1997 Title: Uncoupled phosphorylation and activation in bacterial chemotaxis. The 2.3 A structure of an aspartate to lysine mutant at position 13 of CheY. Authors: Jiang, M. / Bourret, R.B. / Simon, M.I. / Volz, K. #1: Journal: J.Biol.Chem. / Year: 1997 Title: Crystal Structures of Chey Mutants Y106W and T87I/Y106W. Chey Activation Correlates with Movement of Residue 106 Authors: Zhu, X. / Rebello, J. / Matsumura, P. / Volz, K. #2: Journal: J.Biol.Chem. / Year: 1995 Title: Uncoupled Phosphorylation and Activation in Bacterial Chemotaxis. The 2.1-A Structure of a Threonine to Isoleucine Mutant at Position 87 of Chey Authors: Ganguli, S. / Wang, H. / Matsumura, P. / Volz, K. #3: Journal: Biochemistry / Year: 1993 Title: Structural Conservation in the Chey Superfamily Authors: Volz, K. #4: Journal: J.Biol.Chem. / Year: 1991 Title: Crystal Structure of Escherichia Coli Chey Refined at 1.7-A Resolution Authors: Volz, K. / Matsumura, P. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1ehc.cif.gz | 39.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ehc.ent.gz | 26.9 KB | Display | PDB format |
PDBx/mmJSON format | 1ehc.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/eh/1ehc ftp://data.pdbj.org/pub/pdb/validation_reports/eh/1ehc | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 13995.228 Da / Num. of mol.: 1 / Mutation: D13K Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Strain: K12 / Description: NATURALLY-OCCURRING MUTANT / Plasmid: pRBB40.13DK / Production host: Escherichia coli (E. coli) / References: UniProt: P06143, UniProt: P0AE67*PLUS |
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#2: Chemical | ChemComp-SO4 / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.08 Å3/Da / Density % sol: 40.9 % | |||||||||||||||
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Crystal grow | pH: 8.3 / Details: pH 8.3 | |||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / Method: microdialysis / Details: Volz, K., (1986) J.Biol.Chem., 261, 4723. / PH range low: 8.9 / PH range high: 7.4 | |||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 290 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU / Wavelength: 1.5418 |
Detector | Type: SIEMENS / Detector: AREA DETECTOR |
Radiation | Monochromator: GRAPHITE(002) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Highest resolution: 2.26 Å / Num. obs: 5108 / % possible obs: 87.8 % / Observed criterion σ(I): 0 / Rmerge(I) obs: 0.0602 |
Reflection shell | Resolution: 2.26→2.37 Å / % possible all: 24.4 |
Reflection | *PLUS Num. measured all: 12828 |
-Processing
Software |
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Refinement | Method to determine structure: PHASED WITH WT Starting model: MODIFIED WILD-TYPE CHEY Resolution: 2.26→10 Å / σ(F): 2
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Displacement parameters | Biso mean: 15.6 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.2 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.26→10 Å
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Refine LS restraints |
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Software | *PLUS Name: PROFFT / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.143 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |