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- EMDB-1759: Double helical filaments of an N-terminal thioredoxin fusion of TubZ -
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Open data
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Basic information
Entry | Database: EMDB / ID: EMD-1759 | |||||||||
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Title | Double helical filaments of an N-terminal thioredoxin fusion of TubZ | |||||||||
![]() | Double helical filaments of a Thioredoxin N-terminal fusion of TubZ (Q8KNP3_BACTI) from bacillus thuringiensis serovar israelensis (ATCC 35646). density for the thioredoxin fusion of TubZ to remove positive density on the outer boundary of the negative stain and unconnected to the main helix. | |||||||||
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![]() | Cytoskeleton / DNA segregation / FtsZ / FtsZ-like / pBtoxis / pbt156 / plasmid partitioning / RepX / tubulin / tubulin-like / TubZ | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | helical reconstruction / negative staining / Resolution: 35.0 Å | |||||||||
![]() | Aylett CHS / Amos LA / Lowe J | |||||||||
![]() | ![]() Title: Filament structure of bacterial tubulin homologue TubZ. Authors: Christopher H S Aylett / Qing Wang / Katharine A Michie / Linda A Amos / Jan Löwe / ![]() Abstract: Low copy number plasmids often depend on accurate partitioning systems for their continued survival. Generally, such systems consist of a centromere-like region of DNA, a DNA-binding adaptor, and a ...Low copy number plasmids often depend on accurate partitioning systems for their continued survival. Generally, such systems consist of a centromere-like region of DNA, a DNA-binding adaptor, and a polymerizing cytomotive filament. Together these components drive newly replicated plasmids to opposite ends of the dividing cell. The Bacillus thuringiensis plasmid pBToxis relies on a filament of the tubulin/FtsZ-like protein TubZ for its segregation. By combining crystallography and electron microscopy, we have determined the structure of this filament. We explain how GTP hydrolysis weakens the subunit-subunit contact and also shed light on the partitioning of the plasmid-adaptor complex. The double helical superstructure of TubZ filaments is unusual for tubulin-like proteins. Filaments of ParM, the actin-like partitioning protein, are also double helical. We suggest that convergent evolution shapes these different types of cytomotive filaments toward a general mechanism for plasmid separation. | |||||||||
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 | ![]() | 81.8 KB | ![]() | |
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Header (meta data) | ![]() ![]() | 8.5 KB 8.5 KB | Display Display | ![]() |
Images | ![]() | 507.3 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 211 KB | Display | ![]() |
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Full document | ![]() | 210.2 KB | Display | |
Data in XML | ![]() | 4.3 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 | Double helical filaments of a Thioredoxin N-terminal fusion of TubZ (Q8KNP3_BACTI) from bacillus thuringiensis serovar israelensis (ATCC 35646). density for the thioredoxin fusion of TubZ to remove positive density on the outer boundary of the negative stain and unconnected to the main helix. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X: 4.4 Å / Y: 4.4 Å / Z: 4 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 : Double helical filament of Trx-TubZ
Entire | Name: Double helical filament of Trx-TubZ |
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Components |
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-Supramolecule #1000: Double helical filament of Trx-TubZ
Supramolecule | Name: Double helical filament of Trx-TubZ / type: sample / ID: 1000 / Details: Negatively stained / Oligomeric state: Dimer / Number unique components: 1 |
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-Macromolecule #1: Cytomotive filament
Macromolecule | Name: Cytomotive filament / type: protein_or_peptide / ID: 1 / Name.synonym: Cytomotive filament / Oligomeric state: Double filament / Recombinant expression: Yes |
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Source (natural) | Organism: ![]() ![]() |
Recombinant expression | Organism: ![]() ![]() |
-Experimental details
-Structure determination
Method | negative staining |
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![]() | helical reconstruction |
Aggregation state | filament |
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Sample preparation
Concentration | 0.1 mg/mL |
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Buffer | pH: 7.5 Details: 50 mM NaHEPES pH7.5, 150 mM KCl, 5 mM MgCl2 1 mM GTPyS |
Staining | Type: NEGATIVE / Details: 1% Uranyl Acetate |
Grid | Details: CuRh 300 mesh |
Vitrification | Cryogen name: NONE / Instrument: OTHER |
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Electron microscopy
Microscope | FEI TECNAI 12 |
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Image recording | Category: CCD / Film or detector model: KODAK SO-163 FILM / Bits/pixel: 8 |
Electron beam | Acceleration voltage: 120 kV / Electron source: TUNGSTEN HAIRPIN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal magnification: 67000 |
Sample stage | Specimen holder: Eucentric / Specimen holder model: SIDE ENTRY, EUCENTRIC |
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Image processing
Final reconstruction | Applied symmetry - Helical parameters - Axial symmetry: C2 (2 fold cyclic) Algorithm: OTHER / Resolution.type: BY AUTHOR / Resolution: 35.0 Å / Resolution method: OTHER / Software - Name: MRC / Details: Highest resolution map of three |
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