2V0W

N- and C-terminal helices of oat LOV2 (404-546) are involved in light- induced signal transduction (cryo-trapped light structure of LOV2 (404-546))

2V0W の概要

• エントリーDOI: 10.2210/pdb2v0w/pdb
• 関連するPDBエントリー: 2V0U 2V1A 2V1B
• 分子名称: NPH1-1, FLAVIN MONONUCLEOTIDE, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: lov2, kinase, transferase, atp-binding, avena sativa, serine/threonine-protein kinase, phototropin1, light-induced signal transduction, nucleotide-binding
• 由来する生物種: AVENA SATIVA (OAT)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17585.63

構造登録者

Halavaty, A.S.,Moffat, K. (登録日: 2007-05-20, 公開日: 2007-12-11, 最終更新日: 2024-11-06)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.7 Å)