2V1B

N- and C-terminal helices of oat LOV2 (404-546) are involved in light-induced signal transduction (room temperature (293K) light structure of LOV2 (404-546))

Summary for 2V1B

• Entry DOI: 10.2210/pdb2v1b/pdb
• Related: 2V0U 2V0W 2V1A
• Descriptor: NPH1-1, FLAVIN MONONUCLEOTIDE, GLYCEROL, ... (4 entities in total)
• Functional Keywords: lov2, kinase, transferase, atp-binding, avena sativa, serine/threonine-protein kinase, light-induced signal transduction, phototropin1, nucleotide-binding
• Biological source: AVENA SATIVA (OAT)
• Total number of polymer chains: 1
• Total formula weight: 17215.28

Authors

Halavaty, A.S.,Moffat, K. (deposition date: 2007-05-22, release date: 2007-12-11, Last modification date: 2024-11-06)

Primary citation

Halavaty, A.S.,Moffat, K.
N- and C-Terminal Flanking Regions Modulate Light-Induced Signal Transduction in the Lov2 Domain of the Blue Light Sensor Phototropin 1 from Avena Sativa.
Biochemistry, 46:14001-, 2007

PubMed Abstract: Light sensing by photoreceptors controls phototropism, chloroplast movement, stomatal opening, and leaf expansion in plants. Understanding the molecular mechanism by which these processes are regulated requires a quantitative description of photoreceptor dynamics. We focus on a light-driven signal transduction mechanism in the LOV2 domain (LOV, light, oxygen, voltage) of the blue light photoreceptor phototropin 1 from Avena sativa (oat). High-resolution crystal structures of the dark and light states of an oat LOV2 construct including residues Leu404 through Leu546 (LOV2 (404-546)) have been determined at 105 and 293 K. In all four structures, LOV2 (404-546) exhibits the typical Per-ARNT-Sim (PAS) fold, flanked by an additional conserved N-terminal turn-helix-turn motif and a C-terminal flanking region containing an amphipathic Jalpha helix. These regions dock on the LOV2 core domain and bury several hydrophobic residues of the central beta-sheet of the core domain that would otherwise be exposed to solvent. Light structures of LOV2 (404-546) reveal that formation of the covalent bond between Cys450 and the C4a atom of the flavin mononucleotide (FMN) results in local rearrangement of the hydrogen-bonding network in the FMN binding pocket. These rearrangements are associated with disruption of the Asn414-Asp515 hydrogen bond on the surface of the protein and displacement of the N- and C-terminal flanking regions of LOV2 (404-546), both of which constitute a structural signal.

PubMed: 18001137
DOI: 10.1021/BI701543E

Experimental method

X-RAY DIFFRACTION (1.55 Å)