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4RI2

Crystal structure of the photoprotective protein PsbS from spinach

4RI2 の概要
エントリーDOI10.2210/pdb4ri2/pdb
関連するPDBエントリー4RI3
分子名称Photosystem II 22 kDa protein, chloroplastic, nonyl beta-D-glucopyranoside, CHLOROPHYLL A, ... (5 entities in total)
機能のキーワードtransmembrane helices, photo protection, pigment binding, membrane protein
由来する生物種Spinacia oleracea (Spinach)
細胞内の位置Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein: Q02060
タンパク質・核酸の鎖数2
化学式量合計47416.10
構造登録者
Fan, M.,Li, M.,Chang, W. (登録日: 2014-10-05, 公開日: 2015-08-12, 最終更新日: 2024-02-28)
主引用文献Fan, M.,Li, M.,Liu, Z.,Cao, P.,Pan, X.,Zhang, H.,Zhao, X.,Zhang, J.,Chang, W.
Crystal structures of the PsbS protein essential for photoprotection in plants.
Nat.Struct.Mol.Biol., 22:729-735, 2015
Cited by
PubMed Abstract: The photosystem II protein PsbS has an essential role in qE-type nonphotochemical quenching, which protects plants from photodamage under excess light conditions. qE is initiated by activation of PsbS by low pH, but the mechanism of PsbS action remains elusive. Here we report the low-pH crystal structures of PsbS from spinach in its free form and in complex with the qE inhibitor N,N'-dicyclohexylcarbodiimide (DCCD), revealing that PsbS adopts a unique folding pattern, and, unlike other members of the light-harvesting-complex superfamily, it is a noncanonical pigment-binding protein. Structural and biochemical evidence shows that both active and inactive PsbS form homodimers in the thylakoid membranes, and DCCD binding disrupts the lumenal intermolecular hydrogen bonds of the active PsbS dimer. Activation of PsbS by low pH during qE may involve a conformational change associated with altered lumenal intermolecular interactions of the PsbS dimer.
PubMed: 26258636
DOI: 10.1038/nsmb.3068
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.35 Å)
構造検証レポート
Validation report summary of 4ri2
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-12-31に公開中

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