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Yorodumi- EMDB-1160: Double hexameric ring assembly of the type III protein translocas... -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-1160 | |||||||||
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Title | Double hexameric ring assembly of the type III protein translocase ATPase HrcN. | |||||||||
Map data | This volume contains the 3D reconstruction of dodecameric HrcN. It is D6-symmetrized. A threshold of 0.61 is recommended for surface rendering. | |||||||||
Sample |
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Biological species | Pseudomonas syringae pv. phaseolicola (bacteria) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 16.0 Å | |||||||||
Authors | Muller SA / Poyidis C / Stone R / Meesters C / Chami M / Engel A / Economou A / Stahlberg H | |||||||||
Citation | Journal: Mol Microbiol / Year: 2006 Title: Double hexameric ring assembly of the type III protein translocase ATPase HrcN. Authors: Shirley A Müller / Charalambos Pozidis / Remington Stone / Christian Meesters / Mohamed Chami / Andreas Engel / Anastassios Economou / Henning Stahlberg / Abstract: The specialized type III secretion (T3S) apparatus of pathogenic and symbiotic Gram-negative bacteria comprises a complex transmembrane organelle and an ATPase homologous to the F1-ATPase beta ...The specialized type III secretion (T3S) apparatus of pathogenic and symbiotic Gram-negative bacteria comprises a complex transmembrane organelle and an ATPase homologous to the F1-ATPase beta subunit. The T3S ATPase HrcN of Pseudomonas syringae associates with the inner membrane, and its ATP hydrolytic activity is stimulated by dodecamerization. The structure of dodecameric HrcN (HrcN12) determined to 1.6 nm by cryo-electron microscopy is presented. HrcN12 comprises two hexameric rings that are probably stacked face-to-face by the association of their C-terminal domains. It is 11.5 +/- 1.0 nm in diameter, 12.0 +/- 2.0 nm high and has a 2.0-3.8 nm wide inner channel. This structure is compared to a homology model based on the structure of the F1-beta-ATPase. A model for its incorporation within the T3S apparatus is presented. | |||||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | EM map: SurfViewMolmilJmol/JSmol |
Supplemental images |
-Downloads & links
-EMDB archive
Map data | emd_1160.map.gz | 3.4 MB | EMDB map data format | |
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Header (meta data) | emd-1160-v30.xml emd-1160.xml | 8.7 KB 8.7 KB | Display Display | EMDB header |
Images | 1160.gif | 15.9 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-1160 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-1160 | HTTPS FTP |
-Validation report
Summary document | emd_1160_validation.pdf.gz | 218.1 KB | Display | EMDB validaton report |
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Full document | emd_1160_full_validation.pdf.gz | 217.2 KB | Display | |
Data in XML | emd_1160_validation.xml.gz | 4 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-1160 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-1160 | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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-Map
File | Download / File: emd_1160.map.gz / Format: CCP4 / Size: 3.7 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | This volume contains the 3D reconstruction of dodecameric HrcN. It is D6-symmetrized. A threshold of 0.61 is recommended for surface rendering. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 4 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Sample components
-Entire : HrcN
Entire | Name: HrcN |
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Components |
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-Supramolecule #1000: HrcN
Supramolecule | Name: HrcN / type: sample / ID: 1000 Details: The sample had a tendency to aggregate rapidly. Images were usually highly crowded, or empty, from the same cryo-EM grid. Oligomeric state: homododecamer / Number unique components: 1 |
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Molecular weight | Experimental: 601 KDa / Theoretical: 612 KDa / Method: STEM mass measurement |
-Macromolecule #1: HrcN
Macromolecule | Name: HrcN / type: protein_or_peptide / ID: 1 / Name.synonym: HrcN / Number of copies: 12 / Oligomeric state: dodecamer / Recombinant expression: Yes |
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Source (natural) | Organism: Pseudomonas syringae pv. phaseolicola (bacteria) / synonym: Pseudomonas syringae pathovar phaseolicola |
Molecular weight | Experimental: 612 KDa / Theoretical: 601 KDa |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Concentration | 1.0 mg/mL |
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Buffer | pH: 7.4 / Details: 50mM Tris-Cl, pH 7.4, 0.2M NaCl, 20% glycerol |
Grid | Details: Quantifoil 300 mesh |
Vitrification | Cryogen name: ETHANE / Instrument: HOMEMADE PLUNGER / Details: Vitrification instrument: Home-built |
-Electron microscopy
Microscope | FEI/PHILIPS CM200FEG |
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Image recording | Digitization - Scanner: PRIMESCAN / Digitization - Sampling interval: 5.0 µm / Number real images: 165 / Od range: 1 / Bits/pixel: 16 |
Tilt angle max | 0 |
Electron beam | Acceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Calibrated magnification: 50000 / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal magnification: 50000 |
Sample stage | Specimen holder: Eucentric / Specimen holder model: GATAN LIQUID NITROGEN |
-Image processing
CTF correction | Details: SPIDER |
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Final reconstruction | Applied symmetry - Point group: D6 (2x6 fold dihedral) / Resolution.type: BY AUTHOR / Resolution: 16.0 Å / Resolution method: FSC 0.5 CUT-OFF / Software - Name: SPIDER / Number images used: 8742 |
Final two d classification | Number classes: 352 |