|Entry||Database: PDB / ID: 6yt3|
|Title||Structure of the MoStoNano fusion protein|
|Keywords||STRUCTURAL PROTEIN / Fusion protein / crystal engineering / rigid helix / molecular biomimetics|
|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 family active site. / Thioredoxin, conserved site / Thioredoxin domain profile. / Thioredoxin domain / Thioredoxin-like superfamily
Similarity search - Domain/homology
Molybdenum storage protein subunit beta / ADENOSINE-5'-TRIPHOSPHATE / Thioredoxin / Molybdenum storage protein subunit alpha
Similarity search - Component
|Biological species||Azotobacter vinelandii (unknown)|
Salmonella enterica subsp. enterica serovar Bovismorbificans (unknown)
|Method||X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.85 Å|
|Authors||Benoit, R.M. / Bierig, T. / Collu, C. / Engilberge, S. / Olieric, V.|
|Funding support|| Switzerland, 2items |
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.
#1: Journal: Biorxiv / Year: 2020
Title: Chimeric single alpha-helical domains as rigid fusion protein connections for protein nanotechnology and structural biology
Authors: Collu, G. / Bierig, T. / Krebs, A.-S. / Engilberge, S. / Varma, N. / Guixa-Gonzalez, R. / Deupi, X. / Olieric, V. / Poghosyan, E. / Benoit, R.M.
|Structure viewer||Molecule: |
Downloads & links
A: Molybdenum storage protein subunit alpha
B: Thioredoxin,Molybdenum storage protein subunit beta
|Components on special symmetry positions|
|#1: Protein|| |
Mass: 31428.973 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Azotobacter vinelandii (strain DJ / ATCC BAA-1303) (unknown)
Strain: DJ / ATCC BAA-1303 / Gene: mosA, Avin_43200 / Production host: Escherichia coli (E. coli) / References: UniProt: P84308
|#2: Protein|| |
Mass: 40436.559 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Details: chain B has three components that are fused together: Thioredoxin at the N-terminus, then a short EEEKRKREEE rigid helix, then the beta-subunit of MoSto.
Source: (gene. exp.) Salmonella enterica subsp. enterica serovar Bovismorbificans (unknown), (gene. exp.) Azotobacter vinelandii (strain DJ / ATCC BAA-1303) (unknown)
Gene: trxA_2, trxA, A3789_21210, AL561_14185, B7N00_20260, B7N01_17730, B7N34_19660, B7N35_19470, B7N60_21445, B7N72_16575, B7N73_22720, B7N78_20580, B7N79_19980, B7N80_16005, B7N84_20570, B7N95_ ...Gene: trxA_2, trxA, A3789_21210, AL561_14185, B7N00_20260, B7N01_17730, B7N34_19660, B7N35_19470, B7N60_21445, B7N72_16575, B7N73_22720, B7N78_20580, B7N79_19980, B7N80_16005, B7N84_20570, B7N95_20865, CAD68_20095, CBK57_22150, DK062_18215, DOI63_23750, DP779_24195, DPA33_18890, DPK57_04940, DPS13_18845, DPZ52_04610, DRU31_19690, E0916_20730, EJV93_21005, ERS008198_02131, ERS008202_02904, ERS008207_01732, EWC73_19305, EXP31_20825, NCTC5754_04586, mosB, Avin_43210
Strain: DJ / ATCC BAA-1303 / Production host: Escherichia coli (E. coli) / References: UniProt: A0A0U0X1R7, UniProt: P84253
Mass: 507.181 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H16N5O13P3 / Comment: ATP, energy-carrying molecule*YM
|#4: Chemical|| ChemComp-MG / ||#5: Water|| ChemComp-HOH / ||Has ligand of interest||N|
|Experiment||Method: X-RAY DIFFRACTION / Number of used crystals: 1|
|Crystal grow||Temperature: 293 K / Method: vapor diffusion|
Details: 0.1 M tri-Sodium citrate pH 5.6, 10% PEG 4000, 10% Isopropanol
|Diffraction||Mean temperature: 100 K / Serial crystal experiment: N|
|Diffraction source||Source: SYNCHROTRON / Site: SLS / Beamline: X06DA / Wavelength: 1 Å|
|Detector||Type: DECTRIS PILATUS 2M / Detector: PIXEL / Date: May 16, 2019|
|Radiation||Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray|
|Radiation wavelength||Wavelength: 1 Å / Relative weight: 1|
|Reflection||Resolution: 2.85→47.89 Å / Num. obs: 33352 / % possible obs: 99.9 % / Redundancy: 10.6 % / CC1/2: 0.998 / Rpim(I) all: 0.071 / Net I/σ(I): 8.2|
|Reflection shell||Resolution: 2.85→2.98 Å / Mean I/σ(I) obs: 2.3 / Num. unique obs: 1670 / CC1/2: 0.8 / Rpim(I) all: 0.351|
|Refinement||Method to determine structure: MOLECULAR REPLACEMENT|
Starting model: 4F6T
Resolution: 2.85→47.89 Å / Cor.coef. Fo:Fc: 0.871 / Cor.coef. Fo:Fc free: 0.851 / SU R Cruickshank DPI: 0.436 / Cross valid method: THROUGHOUT / σ(F): 0 / SU R Blow DPI: 0.44 / SU Rfree Blow DPI: 0.312 / SU Rfree Cruickshank DPI: 0.315
|Displacement parameters||Biso max: 160.57 Å2 / Biso mean: 65.14 Å2 / Biso min: 3 Å2|
|Refine analyze||Luzzati coordinate error obs: 0.47 Å|
|Refinement step||Cycle: final / Resolution: 2.85→47.89 Å|
|Refine LS restraints|
|LS refinement shell||Resolution: 2.85→2.9 Å / Rfactor Rfree error: 0 / Total num. of bins used: 50 |
|Refinement TLS params.|
Method: refined / Refine-ID: X-RAY DIFFRACTION
|Refinement TLS group|
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