+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-2815 | |||||||||
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Title | FtsAZ constriction in a liposome | |||||||||
Map data | Tomogram of the FtsZ ring reconstituted in liposomes. | |||||||||
Sample |
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Keywords | FtsZ / divisome / bacterial cell division / cytokinesis | |||||||||
Function / homology | Function and homology information FtsZ-dependent cytokinesis / division septum assembly / cell division site / protein polymerization / cytoplasmic side of plasma membrane / cell division / GTPase activity / GTP binding / ATP binding / identical protein binding / cytoplasm Similarity search - Function | |||||||||
Biological species | Thermotoga maritima (bacteria) | |||||||||
Method | electron tomography / cryo EM | |||||||||
Authors | Szwedziak P / Wang Q / Bharat TAM / Tsim M / Lowe J | |||||||||
Citation | Journal: Elife / Year: 2014 Title: Architecture of the ring formed by the tubulin homologue FtsZ in bacterial cell division. Authors: Piotr Szwedziak / Qing Wang / Tanmay A M Bharat / Matthew Tsim / Jan Löwe / Abstract: Membrane constriction is a prerequisite for cell division. The most common membrane constriction system in prokaryotes is based on the tubulin homologue FtsZ, whose filaments in E. coli are anchored ...Membrane constriction is a prerequisite for cell division. The most common membrane constriction system in prokaryotes is based on the tubulin homologue FtsZ, whose filaments in E. coli are anchored to the membrane by FtsA and enable the formation of the Z-ring and divisome. The precise architecture of the FtsZ ring has remained enigmatic. In this study, we report three-dimensional arrangements of FtsZ and FtsA filaments in C. crescentus and E. coli cells and inside constricting liposomes by means of electron cryomicroscopy and cryotomography. In vivo and in vitro, the Z-ring is composed of a small, single-layered band of filaments parallel to the membrane, creating a continuous ring through lateral filament contacts. Visualisation of the in vitro reconstituted constrictions as well as a complete tracing of the helical paths of the filaments with a molecular model favour a mechanism of FtsZ-based membrane constriction that is likely to be accompanied by filament sliding. | |||||||||
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_2815.map.gz | 3.9 MB | EMDB map data format | |
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Header (meta data) | emd-2815-v30.xml emd-2815.xml | 10.5 KB 10.5 KB | Display Display | EMDB header |
Images | emd-2815.png | 252.3 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-2815 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-2815 | HTTPS FTP |
-Related structure data
Related structure data | 2814C C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_2815.map.gz / Format: CCP4 / Size: 10.4 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | Tomogram of the FtsZ ring reconstituted in liposomes. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 17.98 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 : Thermotoga maritima FtsA and FtsZ proteins encapsulated inside li...
Entire | Name: Thermotoga maritima FtsA and FtsZ proteins encapsulated inside liposomes. |
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Components |
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-Supramolecule #1000: Thermotoga maritima FtsA and FtsZ proteins encapsulated inside li...
Supramolecule | Name: Thermotoga maritima FtsA and FtsZ proteins encapsulated inside liposomes. type: sample / ID: 1000 / Number unique components: 2 |
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-Macromolecule #1: FtsZ
Macromolecule | Name: FtsZ / type: protein_or_peptide / ID: 1 / Oligomeric state: polymer / Recombinant expression: Yes |
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Source (natural) | Organism: Thermotoga maritima (bacteria) |
Molecular weight | Theoretical: 38 KDa |
Recombinant expression | Organism: Escherichia coli (E. coli) / Recombinant strain: C41 / Recombinant plasmid: pTXB1 |
Sequence | UniProtKB: Cell division protein FtsZ |
-Macromolecule #2: FtsA
Macromolecule | Name: FtsA / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Oligomeric state: polymer / Recombinant expression: Yes |
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Source (natural) | Organism: Thermotoga maritima (bacteria) |
Molecular weight | Theoretical: 47 KDa |
Recombinant expression | Organism: Escherichia coli (E. coli) / Recombinant strain: C41 / Recombinant plasmid: pTXB1 |
Sequence | UniProtKB: Cell division protein FtsA |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | electron tomography |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.5 / Details: 50 mM Tris 100 mM NaCl 1 mM EDTA 1 mM NaN3 |
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Grid | Details: Quantifoil R2/2 200 mesh Cu/Rh holey carbon grid |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Instrument: FEI VITROBOT MARK III / Method: 3.5 s blot on Whatmann 1 filter paper. |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Calibrated magnification: 26000 / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Cs: 2.7 mm / Nominal defocus max: -10.0 µm / Nominal defocus min: -10.0 µm / Nominal magnification: 26000 |
Specialist optics | Energy filter - Name: Gatan Quantum / Energy filter - Lower energy threshold: 0.0 eV / Energy filter - Upper energy threshold: 20.0 eV |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Tilt series - Axis1 - Min angle: 0 ° / Tilt series - Axis1 - Max angle: 60 ° / Tilt series - Axis1 - Angle increment: 1 ° |
Alignment procedure | Legacy - Astigmatism: Visualisation of power spectrum. |
Date | Aug 29, 2014 |
Image recording | Category: CCD / Film or detector model: GATAN K2 (4k x 4k) / Number real images: 121 / Average electron dose: 150 e/Å2 |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
-Image processing
Final reconstruction | Algorithm: OTHER / Software - Name: IMOD, tomo3D / Number images used: 121 |
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Details | Tilt series data was aligned using IMOD and reconstruction was carried out using tomo3D. |