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Design of stimulus-responsive two-state hinge proteins
Florian Praetorius1,2, Philip J Y Leung1,2,3, Maxx H Tessmer4
1Department of Biochemistry, University of Washington, Seattle, WA, USA.
Science (New York, N.Y.)
|August 17, 2023
Summary
Scientists designed novel "hinge" proteins that switch between two distinct structures based on ligand presence. This breakthrough in protein design offers precise control over protein conformation and binding, mimicking electronic transistors.
Area of Science:
- Biochemistry
- Structural Biology
- Protein Engineering
Background:
- Proteins naturally switch conformations to transduce biochemical signals, similar to transistors in electronics.
- Designing proteins with two stable, distinct structures is a significant challenge in protein engineering.
Purpose of the Study:
- To design novel
- hinge
- proteins capable of switching between two specific conformations.
Main Methods:
- Utilized X-ray crystallography and electron microscopy for structural determination.
- Employed double electron-electron resonance spectroscopy for conformational analysis.
- Performed binding measurements to assess ligand interactions.
Main Results:
- Successfully designed hinge proteins populate distinct states with and without ligand.
- Structural analysis confirmed atomic-level accuracy in designed conformations.
- Conformational changes and binding equilibria were found to be closely coupled.
Conclusions:
- Demonstrated the feasibility of designing proteins with predictable, ligand-controlled conformational switching.
- These engineered proteins offer a platform for precise biochemical information transduction.
- The study advances the field of protein design and synthetic biology.
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