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Structure paper

TitleChimeric single α-helical domains as rigid fusion protein connections for protein nanotechnology and structural biology.
Journal, issue, pagesStructure, Vol. 30, Issue 1, Page 95-106.e7, Year 2022
Publish dateJan 6, 2022
AuthorsGabriella Collu / Tobias Bierig / Anna-Sophia Krebs / Sylvain Engilberge / Niveditha Varma / Ramon Guixà-González / Timothy Sharpe / Xavier Deupi / Vincent Olieric / Emiliya Poghosyan / Roger M Benoit /
PubMed AbstractChimeric 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.
External linksStructure / PubMed:34587504
MethodsEM (single particle) / X-ray diffraction
Resolution1.901 - 2.9 Å
Structure data

EMDB-13292:
Cryo-EM structure of the MoStoNano fusion protein
Method: EM (single particle) / Resolution: 2.9 Å

PDB-6hr1:
Crystal structure of the YFPnano fusion protein
Method: X-RAY DIFFRACTION / Resolution: 1.901 Å

PDB-6xyr:
Structure of the T4Lnano fusion protein
Method: X-RAY DIFFRACTION / Resolution: 2.079 Å

PDB-6yt3:
Structure of the MoStoNano fusion protein
Method: X-RAY DIFFRACTION / Resolution: 2.85 Å

Chemicals

ChemComp-TLA:
L(+)-TARTARIC ACID / Tartaric acid

ChemComp-CA:
Unknown entry

ChemComp-EDO:
1,2-ETHANEDIOL / Ethylene glycol

ChemComp-GOL:
GLYCEROL / Glycerol

ChemComp-NA:
Unknown entry

ChemComp-HOH:
WATER / Water

ChemComp-CL:
Unknown entry / Chloride

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM / Adenosine triphosphate

ChemComp-MG:
Unknown entry

Source
  • Azotobacter vinelandii (bacteria)
  • oryctolagus cuniculus (rabbit)
  • bos taurus (cattle)
  • aequorea victoria (jellyfish)
  • homo sapiens (human)
  • enterobacteria phage t4 (virus)
  • azotobacter vinelandii (strain dj / atcc baa-1303) (bacteria)
  • salmonella enterica subsp. enterica serovar bovismorbificans (bacteria)
KeywordsFusion protein / fluorescent engineered / STRUCTURAL PROTEIN / crystal engineering / rigid helix / molecular biomimetics

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