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Yorodumi- PDB-1ei1: DIMERIZATION OF E. COLI DNA GYRASE B PROVIDES A STRUCTURAL MECHAN... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1ei1 | ||||||
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Title | DIMERIZATION OF E. COLI DNA GYRASE B PROVIDES A STRUCTURAL MECHANISM FOR ACTIVATING THE ATPASE CATALYTIC CENTER | ||||||
Components | DNA GYRASE B | ||||||
Keywords | ISOMERASE / ATPase domain / dimer | ||||||
Function / homology | Function and homology information DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex / DNA negative supercoiling activity / DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity / DNA topoisomerase (ATP-hydrolysing) / DNA topological change / ATP-dependent activity, acting on DNA / DNA-templated DNA replication / chromosome / response to xenobiotic stimulus / response to antibiotic ...DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex / DNA negative supercoiling activity / DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity / DNA topoisomerase (ATP-hydrolysing) / DNA topological change / ATP-dependent activity, acting on DNA / DNA-templated DNA replication / chromosome / response to xenobiotic stimulus / response to antibiotic / DNA-templated transcription / DNA binding / ATP binding / metal ion binding / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 2.3 Å | ||||||
Authors | Brino, L. / Urzhumtsev, A. / Oudet, P. / Moras, D. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2000 Title: Dimerization of Escherichia coli DNA-gyrase B provides a structural mechanism for activating the ATPase catalytic center. Authors: Brino, L. / Urzhumtsev, A. / Mousli, M. / Bronner, C. / Mitschler, A. / Oudet, P. / Moras, D. #1: Journal: Biochimie / Year: 1999 Title: Isoleucine 10 is Essential for DNA Gyrase B Function in Escherichia coli. Authors: Brino, L. / Bronner, C. / Oudet, P. / Mousli, M. #2: Journal: Plasmid / Year: 1997 Title: Expression in Escherichia coli of Y5-mutant and N-terminal Domain-deleted DNA Gyrase B Proteins Affects Strongly Plasmid Maintenance. Authors: Brino, L. / Mousli, M. / Oudet, P. / Weiss, E. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1ei1.cif.gz | 177.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ei1.ent.gz | 138 KB | Display | PDB format |
PDBx/mmJSON format | 1ei1.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ei/1ei1 ftp://data.pdbj.org/pub/pdb/validation_reports/ei/1ei1 | 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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Details | The biological assembly is the dimer composed of chain A and B in the asymmetric unit. |
-Components
#1: Protein | Mass: 43083.457 Da / Num. of mol.: 2 / Fragment: N-TERMINAL 43 KDA FRAGMENT / Mutation: Y5S, Y405S Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) Description: PN43-Y5S (TAC PROMOTER, BETA LACTAMASE GENE, LAC IQ GENE, PBR322 BACKGROUND) Plasmid: PTTQ18 VECTOR(PAG111; PN43-Y5S) / Production host: Escherichia coli (E. coli) References: UniProt: P06982, UniProt: P0AES6*PLUS, EC: 5.99.1.3 #2: Chemical | #3: Chemical | #4: Chemical | #5: 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: 2.66 Å3/Da / Density % sol: 53.82 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 279 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: PEG400, ammonium sulfate, ADPNP, HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 279K | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 120 K |
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Diffraction source | Source: SYNCHROTRON / Site: LURE / Beamline: DW32 / Wavelength: 0.91 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.91 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→15 Å / Num. obs: 33856 / % possible obs: 80 % / Observed criterion σ(F): 3 / Redundancy: 3.4 % / Rmerge(I) obs: 0.044 / Net I/σ(I): 26.4 |
Reflection shell | Resolution: 2.3→2.5 Å / Num. unique all: 33856 / % possible all: 56 |
Reflection | *PLUS Num. measured all: 114762 |
Reflection shell | *PLUS % possible obs: 56 % |
-Processing
Software |
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Refinement | Resolution: 2.3→6 Å / σ(F): 2 / Stereochemistry target values: XPLOR standard
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Refinement step | Cycle: LAST / Resolution: 2.3→6 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Version: 3.1 / Classification: refinement | ||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.3 Å / Lowest resolution: 6 Å / σ(F): 2 / Rfactor obs: 0.171 | ||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||
Refine LS restraints | *PLUS
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