1NP7

Crystal Structure Analysis of Synechocystis sp. PCC6803 cryptochrome

1NP7 の概要

• エントリーDOI: 10.2210/pdb1np7/pdb
• 分子名称: DNA photolyase, SULFATE ION, FLAVIN-ADENINE DINUCLEOTIDE, ... (4 entities in total)
• 機能のキーワード: protein with fad cofactor, lyase
• 由来する生物種: Synechocystis sp.
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 116082.83

構造登録者

Brudler, R.,Hitomi, K.,Daiyasu, H.,Toh, H.,Kucho, K.,Ishiura, M.,Kanehisa, M.,Roberts, V.A.,Todo, T.,Tainer, J.A.,Getzoff, E.D. (登録日: 2003-01-17, 公開日: 2003-01-28, 最終更新日: 2023-08-16)

主引用文献

Brudler, R.,Hitomi, K.,Daiyasu, H.,Toh, H.,Kucho, K.,Ishiura, M.,Kanehisa, M.,Roberts, V.A.,Todo, T.,Tainer, J.A.,Getzoff, E.D.
Identification of a new cryptochrome class: structure, function, and evolution
Mol.Cell, 11:59-67, 2003

PubMed Abstract: Cryptochrome flavoproteins, which share sequence homology with light-dependent DNA repair photolyases, function as photoreceptors in plants and circadian clock components in animals. Here, we coupled sequencing of an Arabidopsis cryptochrome gene with phylogenetic, structural, and functional analyses to identify a new cryptochrome class (cryptochrome DASH) in bacteria and plants, suggesting that cryptochromes evolved before the divergence of eukaryotes and prokaryotes. The cryptochrome crystallographic structure, reported here for Synechocystis cryptochrome DASH, reveals commonalities with photolyases in DNA binding and redox-dependent function, despite distinct active-site and interaction surface features. Whole genome transcriptional profiling together with experimental confirmation of DNA binding indicated that Synechocystis cryptochrome DASH functions as a transcriptional repressor.

PubMed: 12535521
DOI: 10.1016/S1097-2765(03)00008-X

実験手法

X-RAY DIFFRACTION (1.9 Å)