Structural basis of the radical pair state in photolyases and cryptochromes

We present the structure of a photoactivated animal (6-4) photolyase in its radical pair state, captured by serial crystallography. We observe how a conserved asparigine moves towards the semiquinone FAD chromophore and stabilizes it by hydrogen bonding. Several amino acids around the final tryptoph...

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Detalles Bibliográficos
Autores principales: Cellini, Andrea, Shankar, Madan Kumar, Wahlgren, Weixiao Yuan, Nimmrich, Amke, Furrer, Antonia, James, Daniel, Wranik, Maximilian, Aumonier, Sylvain, Beale, Emma V., Dworkowski, Florian, Standfuss, Jörg, Weinert, Tobias, Westenhoff, Sebastian
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Royal Society of Chemistry 2022
Materias:
Chemistry
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9008703/
https://www.ncbi.nlm.nih.gov/pubmed/35352724
http://dx.doi.org/10.1039/d2cc00376g
Descripción
Sumario:We present the structure of a photoactivated animal (6-4) photolyase in its radical pair state, captured by serial crystallography. We observe how a conserved asparigine moves towards the semiquinone FAD chromophore and stabilizes it by hydrogen bonding. Several amino acids around the final tryptophan radical rearrange, opening it up to the solvent. The structure explains how the protein environment stabilizes the radical pair state, which is crucial for function of (6-4) photolyases and cryptochromes.

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