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Updated: Aug 24, 2025

OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy
Published on: February 5, 2020
Shape-Morphing of an Artificial Protein Cage with Unusual Geometry Induced by a Single Amino Acid Change
Mohit Sharma1,2, Artur P Biela1, Agnieszka Kowalczyk1,3
1Malopolska Center of Biotechnology, Jagiellonian University, Gronostajowa 7A, Kraków 30-387, Poland.
Abstract:
Artificial protein cages are constructed from multiple protein subunits. The interaction between the subunits, notably the angle formed between them, controls the geometry of the resulting cage. Here, using the artificial protein cage, "TRAP-cage", we show that a simple alteration in the position of a single amino acid responsible for Au(I)-mediated subunit-subunit interactions in the constituent ring-shaped building blocks results in a more acute dihedral angle between them. In turn, this causes a dramatic shift in the structure from a 24-ring cage with an octahedral symmetry to a 20-ring cage with a C2 symmetry. This symmetry change is accompanied by a decrease in the number of Au(I)-mediated bonds between cysteines and a concomitant change in biophysical properties of the cage.
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