Open AccessShape-Morphing of an Artificial Protein Cage with Unusual Geometry Induced by a Single Amino Acid Change
Author(s) -
Mohit Sharma,
Artur Biela,
Agnieszka Kowalczyk,
Bernard Piette,
Szymon Gaweł,
Philipp Kukura,
Justin L. P. Benesch,
Jonathan G. Heddle
Publication year - 2022
Publication title -
acs nanoscience au
Language(s) - English
Resource type - Journals
ISSN - 2694-2496
DOI - 10.1021/acsnanoscienceau.2c00019
Subject(s) - cage , dihedral angle , morphing , protein subunit , crystallography , ring (chemistry) , geometry , chemistry , symmetry (geometry) , biophysics , biology , combinatorics , mathematics , biochemistry , computer science , hydrogen bond , organic chemistry , molecule , computer vision , gene
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.