4K03

Crystal structure of Drosophila Cryprochrome

4K03 の概要

• エントリーDOI: 10.2210/pdb4k03/pdb
• 関連するPDBエントリー: 4JZY 4K0R
• 分子名称: Cryptochrome-1, FLAVIN-ADENINE DINUCLEOTIDE (3 entities in total)
• 機能のキーワード: rossmann fold, photoreceptor, fad, circadian clock protein
• 由来する生物種: Drosophila melanogaster (Fruit fly)
• 細胞内の位置: Cytoplasm: O77059
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 130289.98

構造登録者

Berndt, A.,Wolf, E. (登録日: 2013-04-03, 公開日: 2013-06-26, 最終更新日: 2024-10-16)

主引用文献

Czarna, A.,Berndt, A.,Singh, H.R.,Grudziecki, A.,Ladurner, A.G.,Timinszky, G.,Kramer, A.,Wolf, E.
Structures of Drosophila cryptochrome and mouse cryptochrome1 provide insight into circadian function.
Cell(Cambridge,Mass.), 153:1394-1405, 2013

PubMed Abstract: Drosophila cryptochrome (dCRY) is a FAD-dependent circadian photoreceptor, whereas mammalian cryptochromes (CRY1/2) are integral clock components that repress mCLOCK/mBMAL1-dependent transcription. We report crystal structures of full-length dCRY, a dCRY loop deletion construct, and the photolyase homology region of mouse CRY1 (mCRY1). Our dCRY structures depict Phe534 of the regulatory tail in the same location as the photolesion in DNA-repairing photolyases and reveal that the sulfur loop and tail residue Cys523 plays key roles in the dCRY photoreaction. Our mCRY1 structure visualizes previously characterized mutations, an NLS, and MAPK and AMPK phosphorylation sites. We show that the FAD and antenna chromophore-binding regions, a predicted coiled-coil helix, the C-terminal lid, and charged surfaces are involved in FAD-independent mPER2 and FBXL3 binding and mCLOCK/mBMAL1 transcriptional repression. The structure of a mammalian cryptochrome1 protein may catalyze the development of CRY chemical probes and the design of therapeutic metabolic modulators.

PubMed: 23746849
DOI: 10.1016/j.cell.2013.05.011

実験手法

X-RAY DIFFRACTION (3.2 Å)