2PR5

Structural Basis for Light-dependent Signaling in the Dimeric LOV Photosensor YtvA (Dark Structure)

2PR5 の概要

• エントリーDOI: 10.2210/pdb2pr5/pdb
• 関連するPDBエントリー: 2PR6
• 分子名称: Blue-light photoreceptor, SODIUM ION, FLAVIN MONONUCLEOTIDE, ... (5 entities in total)
• 機能のキーワード: light-oxygen-voltage, lov, per-arnt-sim, pas, flavoprotein, signaling protein
• 由来する生物種: Bacillus subtilis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 31295.67

構造登録者

Moglich, A.,Moffat, K. (登録日: 2007-05-03, 公開日: 2007-08-07, 最終更新日: 2024-02-21)

主引用文献

Moglich, A.,Moffat, K.
Structural Basis for Light-dependent Signaling in the Dimeric LOV Domain of the Photosensor YtvA.
J.Mol.Biol., 373:112-126, 2007

PubMed Abstract: The photosensor YtvA binds flavin mononucleotide and regulates the general stress reaction in Bacillus subtilis in response to blue light illumination. It belongs to the family of light-oxygen-voltage (LOV) proteins that were first described in plant phototropins and form a subgroup of the Per-Arnt-Sim (PAS) superfamily. Here, we report the three-dimensional structure of the LOV domain of YtvA in its dark and light states. The protein assumes the global fold common to all PAS domains and dimerizes via a hydrophobic interface. Directly C-terminal to the core of the LOV domain, an alpha-helix extends into the solvent. Light absorption causes formation of a covalent bond between a conserved cysteine residue and atom C(4a) of the FMN ring, which triggers rearrangements throughout the LOV domain. Concomitantly, in the dark and light structures, the two subunits of the dimeric protein rotate relative to each other by 5 degrees . This small quaternary structural change is presumably a component of the mechanism by which the activity of YtvA is regulated in response to light. In terms of both structure and signaling mechanism, YtvA differs from plant phototropins and more closely resembles prokaryotic heme-binding PAS domains.

PubMed: 17764689
DOI: 10.1016/j.jmb.2007.07.039

実験手法

X-RAY DIFFRACTION (1.45 Å)