6HR1

Crystal structure of the YFPnano fusion protein

Summary for 6HR1

• Entry DOI: 10.2210/pdb6hr1/pdb
• Descriptor: Myosin light chain kinase 2, skeletal/cardiac muscle,Unconventional myosin-X,Green fluorescent protein,Calmodulin-1, L(+)-TARTARIC ACID, CALCIUM ION, ... (7 entities in total)
• Functional Keywords: fluorescent engineered, structural protein, fusion protein
• Biological source: Oryctolagus cuniculus (Rabbit); More
• Total number of polymer chains: 2
• Total formula weight: 99935.41

Authors

Benoit, R.M. (deposition date: 2018-09-26, release date: 2020-04-08, Last modification date: 2024-10-16)

Primary citation

Collu, G.,Bierig, T.,Krebs, A.S.,Engilberge, S.,Varma, N.,Guixa-Gonzalez, R.,Sharpe, T.,Deupi, X.,Olieric, V.,Poghosyan, E.,Benoit, R.M.
Chimeric single alpha-helical domains as rigid fusion protein connections for protein nanotechnology and structural biology.
Structure, 2021

PubMed 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 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.

PubMed: 34587504
DOI: 10.1016/j.str.2021.09.002

Experimental method

X-RAY DIFFRACTION (1.901 Å)