Disruption of the FMN-A524 interaction cascade and Glu513 induced collapse of the hydrophobic barrier promotes light induced J α-helix unfolding in AsLOV2

This study indicates that the displacement of N492 out of the FMN binding pocket, not necessarily requiring Q513, is essential for the initiation of the Jα-helix unfolding. Rather, the structural reorientation of Q513 activates the protein to cross the hydrophobic barrier and enter the post initiation phase. Similarly, the structural deviations in N482, rather than its integral role in unfolding, could enhance the unfolding rates. Further, the MSM studies on the wild type and the Q513 mutant, provide the spatio-temporal roadmap that layout the possible pathways of structural transition between the dark and the light states of the protein. Overall, the study provides insights useful to enhance the performance of AsLOV2 based photoswitches.PMID:37978801 | DOI:10.1016/j.bpj.2023.11.011
Source: Biophysical Journal - Category: Physics Authors: Source Type: research