|Entry||Database: EMDB / ID: EMD-13292|
|Title||Cryo-EM structure of the MoStoNano fusion protein|
|Map data||The structure of MoStoNano|
|Function / homology|
Function and homology information
glycerol ether metabolic process / nutrient reservoir activity / molybdenum ion binding / protein-disulfide reductase activity / cytoplasm
Similarity search - Function
Molybdenum storage protein subunit alpha/beta / Aspartate/glutamate/uridylate kinase / Amino acid kinase family / Acetylglutamate kinase-like superfamily / Thioredoxin / Thioredoxin / Thioredoxin, conserved site / Thioredoxin family active site. / Thioredoxin domain profile. / Thioredoxin domain / Thioredoxin-like superfamily
Similarity search - Domain/homology
Thioredoxin / Molybdenum storage protein subunit beta / Molybdenum storage protein subunit alpha
Similarity search - Component
|Biological species||Azotobacter vinelandii (unknown)|
|Method||single particle reconstruction / cryo EM / Resolution: 2.9 Å|
|Authors||Benoit RM / Poghosyan E|
|Funding support|| Switzerland, 3 items |
Journal: Structure / Year: 2022
Title: Chimeric single α-helical domains as rigid fusion protein connections for protein nanotechnology and structural biology.
Authors: Gabriella Collu / Tobias Bierig / Anna-Sophia Krebs / Sylvain Engilberge / Niveditha Varma / Ramon Guixà-González / Timothy Sharpe / Xavier Deupi / Vincent Olieric / Emiliya Poghosyan / Roger M Benoit /
Abstract: Chimeric fusion proteins are essential tools for protein nanotechnology. Non-optimized protein-protein connections are usually flexible and therefore unsuitable as structural building blocks. Here we ...Chimeric fusion proteins are essential tools for protein nanotechnology. Non-optimized protein-protein connections are usually flexible and therefore unsuitable as structural building blocks. Here we show that the ER/K motif, a single α-helical domain (SAH), can be seamlessly fused to terminal helices of proteins, forming an extended, partially free-standing rigid helix. This enables the connection of two domains at a defined distance and orientation. We designed three constructs termed YFPnano, T4Lnano, and MoStoNano. Analysis of experimentally determined structures and molecular dynamics simulations reveals a certain degree of plasticity in the connections that allows the adaptation to crystal contact opportunities. Our data show that SAHs can be stably integrated into designed structural elements, enabling new possibilities for protein nanotechnology, for example, to improve the exposure of epitopes on nanoparticles (structural vaccinology), to engineer crystal contacts with minimal impact on construct flexibility (for the study of protein dynamics), and to design novel biomaterials.
|Structure viewer||EM map: |
Downloads & links
|File||Download / File: emd_13292.map.gz / Format: CCP4 / Size: 103 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)|
|Annotation||The structure of MoStoNano|
|Projections & slices|
Images are generated by Spider.
|Voxel size||X=Y=Z: 0.82 Å|
|Symmetry||Space group: 1|
CCP4 map header:
|Projections & Slices|
-Half map: Unfiltered half map after the refinement
|Annotation||Unfiltered half map after the refinement|
|Projections & Slices|
-Half map: Unfiltered half map after the refinement
-Entire : MoStoNano fusion protein
|Entire||Name: MoStoNano fusion protein|
-Supramolecule #1: MoStoNano fusion protein
|Supramolecule||Name: MoStoNano fusion protein / type: complex / ID: 1 / Parent: 0|
|Source (natural)||Organism: Azotobacter vinelandii (unknown)|
|Recombinant expression||Organism: Escherichia coli (E. coli)|
|Processing||single particle reconstruction|
|Grid||Model: UltrAuFoil R1.2/1.3 / Material: GOLD / Mesh: 200|
|Vitrification||Cryogen name: ETHANE / Chamber humidity: 100 % / Instrument: FEI VITROBOT MARK IV|
|Details||The sample was monodisperse.|
|Microscope||FEI TITAN KRIOS|
|Electron beam||Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN|
|Electron optics||Illumination mode: OTHER / Imaging mode: BRIGHT FIELDBright-field microscopy / Cs: 2.7 mm / Nominal magnification: 165000|
|Sample stage||Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN|
|Image recording||Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: COUNTING / Digitization - Dimensions - Width: 3838 pixel / Digitization - Dimensions - Height: 3710 pixel / Number real images: 2472 / Average electron dose: 62.0 e/Å2|
Model: Titan Krios / Image courtesy: FEI Company
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