1np7
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Crystal Structure Analysis of Synechocystis sp. PCC6803 cryptochrome
OverviewOverview
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.
About this StructureAbout this Structure
1NP7 is a Single protein structure of sequence from Synechocystis sp. with SO4 and FAD as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Identification of a new cryptochrome class. Structure, function, and evolution., Brudler R, Hitomi K, Daiyasu H, Toh H, Kucho K, Ishiura M, Kanehisa M, Roberts VA, Todo T, Tainer JA, Getzoff ED, Mol Cell. 2003 Jan;11(1):59-67. PMID:12535521
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