2J4D

Cryptochrome 3 from Arabidopsis thaliana

Summary for 2J4D

• Entry DOI: 10.2210/pdb2j4d/pdb
• Descriptor: CRYPTOCHROME DASH, FLAVIN-ADENINE DINUCLEOTIDE, 5,10-METHENYL-6,7,8-TRIHYDROFOLIC ACID, ... (4 entities in total)
• Functional Keywords: dna-binding protein, cryptochrome, flavoprotein, fad, mitochondrion, plastid, chromophore, chloroplast, transit peptide, blue-light response, dna binding protein
• Biological source: ARABIDOPSIS THALIANA (MOUSE-EAR CRESS)
• Total number of polymer chains: 2
• Total formula weight: 123151.22

Authors

Klar, T.,Pokorny, R.,Batschauer, A.,Essen, L.-O. (deposition date: 2006-08-28, release date: 2007-06-19, Last modification date: 2023-12-13)

Primary citation

Klar, T.,Pokorny, R.,Moldt, J.,Batschauer, A.,Essen, L.-O.
Cryptochrome 3 from Arabidopsis Thaliana: Structural and Functional Analysis of its Complex with a Folate Light Antenna
J.Mol.Biol., 366:954-, 2007

PubMed Abstract: Cryptochromes are almost ubiquitous blue-light receptors and act in several species as central components of the circadian clock. Despite being evolutionary and structurally related with DNA photolyases, a class of light-driven DNA-repair enzymes, and having similar cofactor compositions, cryptochromes lack DNA-repair activity. Cryptochrome 3 from the plant Arabidopsis thaliana belongs to the DASH-type subfamily. Its crystal structure determined at 1.9 Angstroms resolution shows cryptochrome 3 in a dimeric state with the antenna cofactor 5,10-methenyltetrahydrofolate (MTHF) bound in a distance of 15.2 Angstroms to the U-shaped FAD chromophore. Spectroscopic studies on a mutant where a residue crucial for MTHF-binding, E149, was replaced by site-directed mutagenesis demonstrate that MTHF acts in cryptochrome 3 as a functional antenna for the photoreduction of FAD.

PubMed: 17188299
DOI: 10.1016/J.JMB.2006.11.066

Experimental method

X-RAY DIFFRACTION (1.9 Å)