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Updated: Jan 25, 2026

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation
Published on: October 4, 2024
Computational Design and Study of Artificial Selenoenzyme with Controllable Activity Based on an Allosteric Protein
Siyuan Li1, Wanjia Xu1, Shengnan Chu1
1State Key Laboratory of Supramolecular Structure and Materials, Institute of Theoretical Chemistry, Jilin University, 2699 Qianjin Road, Changchun, 130012, China.
Abstract:
The establishment of new enzymatic function in an existing scaffold is a great challenge for protein engineers. In previous work, a highly efficient artificial selenoenzyme with controllable activity was constructed, based on a Ca2+ -responsive recoverin (Rn) protein. In this study, a design strategy combining docking, molecular dynamics, and MM-PBSA is presented, to predict the catalytically active site of glutathione peroxidase (GPx) on the allosteric domain of Rn. The energy contributions of the binding hot spot residues are evaluated further by energy decomposition analysis to determine the detailed substrate recognition mechanism of Rn, which provides clear guidance for artificial enzyme design for improved substrate binding (Michaelis-Menten constant, Km ).
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