+Open data
-Basic information
Entry | Database: PDB / ID: 4s0r | ||||||
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Title | Structure of GS-TnrA complex | ||||||
Components |
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Keywords | Ligase / chaperone / glutamine synthesis / transcription regulation | ||||||
Function / homology | Function and homology information nitrogen catabolite activation of transcription / cellular response to nitrogen levels / glutamine binding / nitrogen catabolite repression of transcription / negative regulation of core promoter binding / glutamine synthetase / glutamine biosynthetic process / glutamine synthetase activity / glutamate binding / core promoter sequence-specific DNA binding ...nitrogen catabolite activation of transcription / cellular response to nitrogen levels / glutamine binding / nitrogen catabolite repression of transcription / negative regulation of core promoter binding / glutamine synthetase / glutamine biosynthetic process / glutamine synthetase activity / glutamate binding / core promoter sequence-specific DNA binding / DNA-binding transcription factor binding / negative regulation of DNA-templated transcription / magnesium ion binding / ATP binding / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | Bacillus subtilis (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.5 Å | ||||||
Authors | Schumacher, M.A. / Chinnam, N.G. / Cuthbert, B. / Tonthat, N.K. | ||||||
Citation | Journal: Genes Dev. / Year: 2015 Title: Structures of regulatory machinery reveal novel molecular mechanisms controlling B. subtilis nitrogen homeostasis. Authors: Schumacher, M.A. / Chinnam, N.B. / Cuthbert, B. / Tonthat, N.K. / Whitfill, T. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4s0r.cif.gz | 1.2 MB | Display | PDBx/mmCIF format |
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PDB format | pdb4s0r.ent.gz | 1 MB | Display | PDB format |
PDBx/mmJSON format | 4s0r.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/s0/4s0r ftp://data.pdbj.org/pub/pdb/validation_reports/s0/4s0r | HTTPS FTP |
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-Related 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: 50620.379 Da / Num. of mol.: 14 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bacillus subtilis (bacteria) / Strain: 168 / Gene: glnA, BSU17460 / Production host: Escherichia coli (E. coli) / References: UniProt: P12425, glutamine synthetase #2: Protein/peptide | Mass: 1897.188 Da / Num. of mol.: 14 / Source method: obtained synthetically / References: UniProt: Q45666*PLUS #3: Chemical | ChemComp-GLN / #4: Chemical | ChemComp-MG / |
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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: 3.56 Å3/Da / Density % sol: 65.44 % |
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Crystal grow | Temperature: 298 K / pH: 6.5 Details: 25% PEG 400, MES, pH 6.5, 5% PEG 8000, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ALS / Beamline: 8.3.1 / Wavelength: 1 |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Mar 4, 2014 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 3.5→147.9 Å / Num. obs: 118362 / Observed criterion σ(I): 0 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 3.5→147.9 Å / σ(F): 0 / Stereochemistry target values: ENGH & HUBER
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Refinement step | Cycle: LAST / Resolution: 3.5→147.9 Å
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