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5ZM0

X-ray structure of animal-like Cryptochrome from Chlamydomonas reinhardtii

Summary for 5ZM0
Entry DOI10.2210/pdb5zm0/pdb
DescriptorCryptochrome photoreceptor, FLAVIN-ADENINE DINUCLEOTIDE, GLYCEROL, ... (6 entities in total)
Functional Keywordscryptochrome, photolyase, photoreceptor, flavoprotein
Biological sourceChlamydomonas reinhardtii (Chlamydomonas smithii)
Total number of polymer chains1
Total formula weight59595.51
Authors
Franz, S.,Ignatz, E.,Wenzel, S.,Zielosko, H.,Gusti Ngurah Putu, E.P.,Maestre-Reyna, M.,Tsai, M.-D.,Yamamoto, J.,Mittag, M.,Essen, L.-O. (deposition date: 2018-03-31, release date: 2018-07-25, Last modification date: 2023-11-22)
Primary citationFranz, 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: 30032195
DOI: 10.1093/nar/gky621
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.6 Å)
Structure validation

226707

數據於2024-10-30公開中

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