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A hinge migration mechanism unlocks the evolution of green-to-red photoconversion in GFP-like proteins. | LitMetric

A hinge migration mechanism unlocks the evolution of green-to-red photoconversion in GFP-like proteins.

Structure

Department of Chemistry and Biochemistry, Arizona State University, Tempe, AZ 85287, USA; Center for Bioenergy and Photosynthesis, Arizona State University, Tempe, AZ 85287, USA. Electronic address:

Published: January 2015

In proteins, functional divergence involves mutations that modify structure and dynamics. Here we provide experimental evidence for an evolutionary mechanism driven solely by long-range dynamic motions without significant backbone adjustments, catalytic group rearrangements, or changes in subunit assembly. Crystallographic structures were determined for several reconstructed ancestral proteins belonging to a GFP class frequently employed in superresolution microscopy. Their chain flexibility was analyzed using molecular dynamics and perturbation response scanning. The green-to-red photoconvertible phenotype appears to have arisen from a common green ancestor by migration of a knob-like anchoring region away from the active site diagonally across the β barrel fold. The allosterically coupled mutational sites provide active site conformational mobility via epistasis. We propose that light-induced chromophore twisting is enhanced in a reverse-protonated subpopulation, activating internal acid-base chemistry and backbone cleavage to enlarge the chromophore. Dynamics-driven hinge migration may represent a more general platform for the evolution of novel enzyme activities.

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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4370283PMC
http://dx.doi.org/10.1016/j.str.2014.11.011DOI Listing

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