Structural highlights
Publication Abstract from PubMed
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.
Structural basis of the radical pair state in photolyases and cryptochromes.,Cellini A, Shankar MK, Wahlgren WY, Nimmrich A, Furrer A, James D, Wranik M, Aumonier S, Beale EV, Dworkowski F, Standfuss J, Weinert T, Westenhoff S Chem Commun (Camb). 2022 Mar 30. doi: 10.1039/d2cc00376g. PMID:35352724[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Cellini A, Shankar MK, Wahlgren WY, Nimmrich A, Furrer A, James D, Wranik M, Aumonier S, Beale EV, Dworkowski F, Standfuss J, Weinert T, Westenhoff S. Structural basis of the radical pair state in photolyases and cryptochromes. Chem Commun (Camb). 2022 Mar 30. doi: 10.1039/d2cc00376g. PMID:35352724 doi:http://dx.doi.org/10.1039/d2cc00376g
