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Yorodumi- EMDB-8500: Subtomogram average of the non-piliated toxin-coregulated pilus m... -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-8500 | |||||||||
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Title | Subtomogram average of the non-piliated toxin-coregulated pilus machine in Vibrio cholerae cells with tcpD knockout (aligning OM-parts) | |||||||||
Map data | Subtomogram average of the non-piliated toxin-coregulated pilus machine in Vibrio cholerae cells with tcpD knockout (aligning OM-parts) | |||||||||
Sample |
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Biological species | Vibrio cholerae (bacteria) | |||||||||
Method | subtomogram averaging / cryo EM / Resolution: 50.0 Å | |||||||||
Authors | Chang Y-W / Kjaer A / Jensen GJ | |||||||||
Citation | Journal: Nat Microbiol / Year: 2017 Title: Architecture of the Vibrio cholerae toxin-coregulated pilus machine revealed by electron cryotomography. Authors: Yi-Wei Chang / Andreas Kjær / Davi R Ortega / Gabriela Kovacikova / John A Sutherland / Lee A Rettberg / Ronald K Taylor / Grant J Jensen / Abstract: Type IV pili (T4P) are filamentous appendages found on many Bacteria and Archaea. They are helical fibres of pilin proteins assembled by a multi-component macromolecular machine we call the basal ...Type IV pili (T4P) are filamentous appendages found on many Bacteria and Archaea. They are helical fibres of pilin proteins assembled by a multi-component macromolecular machine we call the basal body. Based on pilin features, T4P are classified into type IVa pili (T4aP) and type IVb pili (T4bP). T4aP are more widespread and are involved in cell motility, DNA transfer, host predation and electron transfer. T4bP are less prevalent and are mainly found in enteropathogenic bacteria, where they play key roles in host colonization. Following similar work on T4aP machines, here we use electron cryotomography to reveal the three-dimensional in situ structure of a T4bP machine in its piliated and non-piliated states. The specific machine we analyse is the Vibrio cholerae toxin-coregulated pilus machine (TCPM). Although only about half of the components of the TCPM show sequence homology to components of the previously analysed Myxococcus xanthus T4aP machine (T4aPM), we find that their structures are nevertheless remarkably similar. Based on homologies with components of the M. xanthus T4aPM and additional reconstructions of TCPM mutants in which the non-homologous proteins are individually deleted, we propose locations for all eight TCPM components within the complex. Non-homologous proteins in the T4aPM and TCPM are found to form similar structures, suggesting new hypotheses for their functions and evolutionary histories. | |||||||||
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_8500.map.gz | 1.2 MB | EMDB map data format | |
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Header (meta data) | emd-8500-v30.xml emd-8500.xml | 10.8 KB 10.8 KB | Display Display | EMDB header |
Images | emd_8500.png | 39.5 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-8500 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-8500 | HTTPS FTP |
-Validation report
Summary document | emd_8500_validation.pdf.gz | 78.6 KB | Display | EMDB validaton report |
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Full document | emd_8500_full_validation.pdf.gz | 77.7 KB | Display | |
Data in XML | emd_8500_validation.xml.gz | 493 B | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-8500 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-8500 | HTTPS FTP |
-Related structure data
Related structure data | 3792C 8492C 8493C 8494C 8495C 8496C 8497C 8498C 8499C 8501C 8502C 8503C C: citing same article (ref.) |
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Similar structure data |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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-Map
File | Download / File: emd_8500.map.gz / Format: CCP4 / Size: 1.4 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | Subtomogram average of the non-piliated toxin-coregulated pilus machine in Vibrio cholerae cells with tcpD knockout (aligning OM-parts) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. generated in cubic-lattice coordinate | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 7.8 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 : Toxin-coregulated pilus machine
Entire | Name: Toxin-coregulated pilus machine |
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Components |
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-Supramolecule #1: Toxin-coregulated pilus machine
Supramolecule | Name: Toxin-coregulated pilus machine / type: complex / ID: 1 / Parent: 0 |
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Source (natural) | Organism: Vibrio cholerae (bacteria) |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | subtomogram averaging |
Aggregation state | cell |
-Sample preparation
Buffer | pH: 7 |
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Vitrification | Cryogen name: ETHANE-PROPANE |
-Electron microscopy
Microscope | FEI POLARA 300 |
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Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 1.5 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |
Experimental equipment | Model: Tecnai Polara / Image courtesy: FEI Company |