6FN3
X-ray structure of animal-like Cryptochrome from Chlamydomonas reinhardtii
Summary for 6FN3
Entry DOI | 10.2210/pdb6fn3/pdb |
Descriptor | Cryptochrome photoreceptor, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, FLAVIN-ADENINE DINUCLEOTIDE, ... (6 entities in total) |
Functional Keywords | cryptochrome, photolyase, photoreceptor, flavoprotein |
Biological source | Chlamydomonas reinhardtii (Chlamydomonas smithii) |
Total number of polymer chains | 1 |
Total formula weight | 59895.86 |
Authors | Franz, S.,Ignatz, E.,Wenzel, S.,Zielosko, H.,Yamamoto, J.,Mittag, M.,Essen, L.-O. (deposition date: 2018-02-02, release date: 2018-08-01, Last modification date: 2024-05-08) |
Primary citation | Franz, S.,Ignatz, E.,Wenzel, S.,Zielosko, H.,Putu, E.P.G.N.,Maestre-Reyna, M.,Tsai, M.D.,Yamamoto, J.,Mittag, M.,Essen, L.O. Structure of the bifunctional cryptochrome aCRY from Chlamydomonas reinhardtii. Nucleic Acids Res., 46:8010-8022, 2018 Cited by PubMed Abstract: Photolyases and cryptochromes form an almost ubiquitous family of blue light photoreceptors involved in the repair and maintenance of DNA integrity or regulatory control. We found that one cryptochrome from the green alga Chlamydomonas reinhardtii (CraCRY) is capable of both, control of transcript levels and the sexual cycle of the alga in a positive (germination) and negative manner (mating ability), as well as catalyzing the repair of UV-DNA lesions. Its 1.6 Å crystal structure shows besides the FAD chromophore an aromatic tetrad that is indispensable in animal-like type I cryptochromes for light-driven change of their signaling-active redox state and formation of a stable radical pair. Given CraCRY's catalytic activity as (6-4) photolyase in vivo and in vitro, we present the first co-crystal structure of a cryptochrome with duplex DNA comprising a (6-4) pyrimidine-pyrimidone lesion. This 2.9 Å structure reveals a distinct conformation for the catalytic histidine His1, H357, that challenges previous models of a single-photon driven (6-4) photolyase mechanism. PubMed: 30032195DOI: 10.1093/nar/gky621 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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