5A8B

Structure of a parallel dimer of the aureochrome 1a LOV domain from Phaeodactylum tricornutum

5A8B の概要

• エントリーDOI: 10.2210/pdb5a8b/pdb
• 関連するPDBエントリー: 5A8I 5A8J
• 分子名称: PTAUREO1A LOV2 DOMAIN, FLAVIN MONONUCLEOTIDE, CHLORIDE ION, ... (5 entities in total)
• 機能のキーワード: unknown function, aureochrome 1, parallel lov dimer and flanking helix.
• 由来する生物種: PHAEODACTYLUM TRICORNUTUM
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 73955.61

構造登録者

Banerjee, A.,Herman, E.,Kottke, T.,Essen, L.O. (登録日: 2015-07-14, 公開日: 2016-02-10, 最終更新日: 2024-01-10)

主引用文献

Banerjee, A.,Herman, E.,Kottke, T.,Essen, L.O.
Structure of a Native-Like Aureochrome 1A Lov Domain Dimer from Phaeodactylum Tricornutum.
Structure, 24:171-, 2016

PubMed Abstract: Light-oxygen-voltage (LOV) domains absorb blue light for mediating various biological responses in all three domains of life. Aureochromes from stramenopile algae represent a subfamily of photoreceptors that differs by its inversed topology with a C-terminal LOV sensor and an N-terminal effector (basic region leucine zipper, bZIP) domain. We crystallized the LOV domain including its flanking helices, A'α and Jα, of aureochrome 1a from Phaeodactylum tricornutum in the dark state and solved the structure at 2.8 Å resolution. Both flanking helices contribute to the interface of the native-like dimer. Small-angle X-ray scattering shows light-induced conformational changes limited to the dimeric envelope as well as increased flexibility in the lit state for the flanking helices. These rearrangements are considered to be crucial for the formation of the light-activated dimer. Finally, the LOV domain of the class 2 aureochrome PtAUREO2 was shown to lack a chromophore because of steric hindrance caused by M301.

PubMed: 26688213
DOI: 10.1016/J.STR.2015.10.022

実験手法

X-RAY DIFFRACTION (2.791 Å)