1JNU

Photoexcited structure of the plant photoreceptor domain, phy3 LOV2

Summary for 1JNU

• Entry DOI: 10.2210/pdb1jnu/pdb
• Related: 1BYW 1DRM 1G28 2PHY
• Descriptor: PHY3 PROTEIN, FLAVIN MONONUCLEOTIDE (3 entities in total)
• Functional Keywords: cysteinyl-flavin adduct, photoexcited, pas, lov, plant photoreceptor, phototropin, photochemistry, light-driven bond, phy3, signaling protein, electron transport
• Biological source: Adiantum capillus-veneris
• Total number of polymer chains: 4
• Total formula weight: 50552.43

Authors

Crosson, S.,Moffat, K. (deposition date: 2001-07-25, release date: 2002-06-14, Last modification date: 2024-11-13)

Primary citation

Crosson, S.,Moffat, K.
Photoexcited structure of a plant photoreceptor domain reveals a light-driven molecular switch.
Plant Cell, 14:1067-1075, 2002

PubMed Abstract: The phototropins are flavoprotein kinases that control phototropic bending, light-induced chloroplast movement, and stomatal opening in plants. Two flavin mononucleotide binding light, oxygen, or voltage (LOV) domains are the sites for initial photochemistry in these blue light photoreceptors. We have determined the steady state, photoexcited crystal structure of a flavin-bound LOV domain. The structure reveals a unique photochemical switch in the flavin binding pocket in which the absorption of light drives the formation of a reversible covalent bond between a highly conserved Cys residue and the flavin cofactor. This provides a molecular picture of a cysteinyl-flavin covalent adduct, the presumed signaling species that leads to phototropin kinase activation and subsequent signal transduction. We identify closely related LOV domains in two eubacterial proteins that suggests the light-induced conformational change evident in this structure is an ancient biomolecular response to light, arising before the appearance of plants.

PubMed: 12034897
DOI: 10.1105/tpc.010475

Experimental method

X-RAY DIFFRACTION (2.6 Å)