1U3C
Crystal Structure of the PHR domain of Cryptochrome 1 from Arabidopsis thaliana
1U3C の概要
エントリーDOI | 10.2210/pdb1u3c/pdb |
関連するPDBエントリー | 1u3d |
分子名称 | Cryptochrome 1 apoprotein, MAGNESIUM ION, CHLORIDE ION, ... (7 entities in total) |
機能のキーワード | photolyase, amppnp, signaling protein |
由来する生物種 | Arabidopsis thaliana (thale cress) |
細胞内の位置 | Cytoplasm: Q43125 |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 58807.25 |
構造登録者 | Brautigam, C.A.,Smith, B.S.,Ma, Z.,Palnitkar, M.,Tomchick, D.R.,Machius, M.,Deisenhofer, J. (登録日: 2004-07-21, 公開日: 2004-08-24, 最終更新日: 2024-11-20) |
主引用文献 | Brautigam, C.A.,Smith, B.S.,Ma, Z.,Palnitkar, M.,Tomchick, D.R.,Machius, M.,Deisenhofer, J. Structure of the photolyase-like domain of cryptochrome 1 from Arabidopsis thaliana. Proc.Natl.Acad.Sci.USA, 101:12142-12147, 2004 Cited by PubMed Abstract: Signals generated by cryptochrome (CRY) blue-light photoreceptors are responsible for a variety of developmental and circadian responses in plants. The CRYs are also identified as circadian blue-light photoreceptors in Drosophila and components of the mammalian circadian clock. These flavoproteins all have an N-terminal domain that is similar to photolyase, and most have an additional C-terminal domain of variable length. We present here the crystal structure of the photolyase-like domain of CRY-1 from Arabidopsis thaliana. The structure reveals a fold that is very similar to photolyase, with a single molecule of FAD noncovalently bound to the protein. The surface features of the protein and the dissimilarity of a surface cavity to that of photolyase account for its lack of DNA-repair activity. Previous in vitro experiments established that the photolyase-like domain of CRY-1 can bind Mg.ATP, and we observe a single molecule of an ATP analog bound in the aforementioned surface cavity, near the bound FAD cofactor. The structure has implications for the signaling mechanism of CRY blue-light photoreceptors. PubMed: 15299148DOI: 10.1073/pnas.0404851101 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.6 Å) |
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