7DJM

Structure of four truncated and mutated forms of quenching protein

7DJM の概要

• エントリーDOI: 10.2210/pdb7djm/pdb
• 分子名称: Protein SUPPRESSOR OF QUENCHING 1, chloroplastic, ACETATE ION, 2,3-DIHYDROXY-1,4-DITHIOBUTANE, ... (5 entities in total)
• 機能のキーワード: suppressor, quenching, plant protein
• 由来する生物種: Arabidopsis thaliana (thale cress)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 54418.81

構造登録者

Yu, G.M.,Pan, X.W.,Li, M. (登録日: 2020-11-20, 公開日: 2022-06-08, 最終更新日: 2023-11-29)

主引用文献

Yu, G.,Hao, J.,Pan, X.,Shi, L.,Zhang, Y.,Wang, J.,Fan, H.,Xiao, Y.,Yang, F.,Lou, J.,Chang, W.,Malnoe, A.,Li, M.
Structure of Arabidopsis SOQ1 lumenal region unveils C-terminal domain essential for negative regulation of photoprotective qH.
Nat.Plants, 8:840-855, 2022

PubMed Abstract: Non-photochemical quenching (NPQ) plays an important role for phototrophs in decreasing photo-oxidative damage. qH is a sustained form of NPQ and depends on the plastid lipocalin (LCNP). A thylakoid membrane-anchored protein SUPPRESSOR OF QUENCHING1 (SOQ1) prevents qH formation by inhibiting LCNP. SOQ1 suppresses qH with its lumen-located thioredoxin (Trx)-like and NHL domains. Here we report structural data, genetic modification and biochemical characterization of Arabidopsis SOQ1 lumenal domains. Our results show that the Trx-like and NHL domains are associated together, with the cysteine motif located at their interface. Residue E859, required for SOQ1 function, is pivotal for maintaining the Trx-NHL association. Importantly, the C-terminal region of SOQ1 forms an independent β-stranded domain that has structural homology to the N-terminal domain of bacterial disulfide bond protein D and is essential for negative regulation of qH. Furthermore, SOQ1 is susceptible to cleavage at the loops connecting the neighbouring lumenal domains both in vitro and in vivo, which could be a regulatory process for its suppression function of qH.

PubMed: 35798975
DOI: 10.1038/s41477-022-01177-z

実験手法

X-RAY DIFFRACTION (1.70000117792 Å)