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- EMDB-1504: Structural basis for the regulated protease and chaperone functio... -
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Open data
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Basic information
Entry | Database: EMDB / ID: EMD-1504 | |||||||||
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Title | Structural basis for the regulated protease and chaperone function of DegP | |||||||||
![]() | negative stain EM structure of the DegP24-OMP complex | |||||||||
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![]() | protease-chaperone / electron microscopy / single particle analysis | |||||||||
Function / homology | ![]() peptidase Do / programmed cell death / response to temperature stimulus / protein quality control for misfolded or incompletely synthesized proteins / chaperone-mediated protein folding / serine-type peptidase activity / protein folding / peptidase activity / response to heat / outer membrane-bounded periplasmic space ...peptidase Do / programmed cell death / response to temperature stimulus / protein quality control for misfolded or incompletely synthesized proteins / chaperone-mediated protein folding / serine-type peptidase activity / protein folding / peptidase activity / response to heat / outer membrane-bounded periplasmic space / response to oxidative stress / periplasmic space / positive regulation of apoptotic process / serine-type endopeptidase activity / proteolysis / identical protein binding / plasma membrane Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | single particle reconstruction / negative staining / Resolution: 23.0 Å | |||||||||
![]() | Krojer T / Sawa J / Schaefer E / Saibil HR / Ehrmann M / Clausen T | |||||||||
![]() | ![]() Title: Structural basis for the regulated protease and chaperone function of DegP. Authors: Tobias Krojer / Justyna Sawa / Eva Schäfer / Helen R Saibil / Michael Ehrmann / Tim Clausen / ![]() Abstract: All organisms have to monitor the folding state of cellular proteins precisely. The heat-shock protein DegP is a protein quality control factor in the bacterial envelope that is involved in ...All organisms have to monitor the folding state of cellular proteins precisely. The heat-shock protein DegP is a protein quality control factor in the bacterial envelope that is involved in eliminating misfolded proteins and in the biogenesis of outer-membrane proteins. Here we describe the molecular mechanisms underlying the regulated protease and chaperone function of DegP from Escherichia coli. We show that binding of misfolded proteins transforms hexameric DegP into large, catalytically active 12-meric and 24-meric multimers. A structural analysis of these particles revealed that DegP represents a protein packaging device whose central compartment is adaptable to the size and concentration of substrate. Moreover, the inner cavity serves antagonistic functions. Whereas the encapsulation of folded protomers of outer-membrane proteins is protective and might allow safe transit through the periplasm, misfolded proteins are eliminated in the molecular reaction chamber. Oligomer reassembly and concomitant activation on substrate binding may also be critical in regulating other HtrA proteases implicated in protein-folding diseases. | |||||||||
History |
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Structure visualization
Movie |
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Structure viewer | EM map: ![]() ![]() ![]() |
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 7.9 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 6.9 KB 6.9 KB | Display Display | ![]() |
Images | ![]() | 77.5 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 228 KB | Display | ![]() |
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Full document | ![]() | 227.2 KB | Display | |
Data in XML | ![]() | 5.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
EMDB pages | ![]() ![]() |
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Map
File | ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | negative stain EM structure of the DegP24-OMP complex | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 4.44 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
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Sample components
-Entire : proteolytically inactive DegP24mer with bound Omp protein
Entire | Name: proteolytically inactive DegP24mer with bound Omp protein |
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Components |
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-Supramolecule #1000: proteolytically inactive DegP24mer with bound Omp protein
Supramolecule | Name: proteolytically inactive DegP24mer with bound Omp protein type: sample / ID: 1000 / Details: monodisperse sample / Oligomeric state: 24mer / Number unique components: 2 |
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Molecular weight | Experimental: 1.13 MDa |
-Macromolecule #1: protease
Macromolecule | Name: protease / type: protein_or_peptide / ID: 1 / Name.synonym: DegP Details: proteolytically inactive DegP24mer with bound Omp protein Number of copies: 1 / Oligomeric state: 24 / Recombinant expression: Yes |
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Source (natural) | Organism: ![]() ![]() |
-Experimental details
-Structure determination
Method | negative staining |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Concentration | 0.0064 mg/mL |
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Staining | Type: NEGATIVE Details: negatively stained with 2% (w/v) uranyl acetate on glow discharged, carbon-coated grids |
Vitrification | Cryogen name: NONE / Instrument: OTHER |
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Electron microscopy
Microscope | FEI TECNAI F20 |
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Electron beam | Acceleration voltage: 200 kV / Electron source: ![]() |
Electron optics | Illumination mode: OTHER / Imaging mode: OTHER |
Sample stage | Specimen holder: single tilt / Specimen holder model: OTHER |
Experimental equipment | ![]() Model: Tecnai F20 / Image courtesy: FEI Company |
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Image processing
Final reconstruction | Applied symmetry - Point group: O (octahedral) / Resolution.type: BY AUTHOR / Resolution: 23.0 Å / Resolution method: FSC 0.5 CUT-OFF Details: octahedral symmetry was used for the reconstruction |
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