1NP7

Crystal Structure Analysis of Synechocystis sp. PCC6803 cryptochrome

Summary for 1NP7

• Entry DOI: 10.2210/pdb1np7/pdb
• Descriptor: DNA photolyase, SULFATE ION, FLAVIN-ADENINE DINUCLEOTIDE, ... (4 entities in total)
• Functional Keywords: protein with fad cofactor, lyase
• Biological source: Synechocystis sp.
• Total number of polymer chains: 2
• Total formula weight: 116082.83

Authors

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. (deposition date: 2003-01-17, release date: 2003-01-28, Last modification date: 2023-08-16)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.9 Å)