3QV1

Crystal structure of the binary complex of photosyntetic A4 glyceraldehyde 3-phosphate dehydrogenase (GAPDH) with cp12-2, both from Arabidopsis thaliana.

3QV1 の概要

• エントリーDOI: 10.2210/pdb3qv1/pdb
• 関連するPDBエントリー: 3K2B
• 分子名称: Glyceraldehyde-3-phosphate dehydrogenase A, chloroplastic, CP12 protein, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ... (7 entities in total)
• 機能のキーワード: rossmann fold, calvin cycle, nad, chloroplast, oxidoreductase-protein binding complex, oxidoreductase/protein binding
• 由来する生物種: Arabidopsis thaliana (mouse-ear cress,thale-cress); 詳細
• 細胞内の位置: Plastid, chloroplast membrane; Peripheral membrane protein: P25856; Plastid, chloroplast : Q9LZP9
• タンパク質・核酸の鎖数: 9
• 化学式量合計: 249165.63

構造登録者

Thumiger, A.,Fermani, S.,Falini, G.,Marri, L.,Sparla, F.,Trost, P. (登録日: 2011-02-25, 公開日: 2012-02-29, 最終更新日: 2024-11-06)

主引用文献

Fermani, S.,Trivelli, X.,Sparla, F.,Thumiger, A.,Calvaresi, M.,Marri, L.,Falini, G.,Zerbetto, F.,Trost, P.
Conformational Selection and Folding-upon-binding of Intrinsically Disordered Protein CP12 Regulate Photosynthetic Enzymes Assembly.
J.Biol.Chem., 287:21372-21383, 2012

PubMed Abstract: Carbon assimilation in plants is regulated by the reduction of specific protein disulfides by light and their re-oxidation in the dark. The redox switch CP12 is an intrinsically disordered protein that can form two disulfide bridges. In the dark oxidized CP12 forms an inactive supramolecular complex with glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and phosphoribulokinase, two enzymes of the carbon assimilation cycle. Here we show that binding of CP12 to GAPDH, the first step of ternary complex formation, follows an integrated mechanism that combines conformational selection with induced folding steps. Initially, a CP12 conformation characterized by a circular structural motif including the C-terminal disulfide is selected by GAPDH. Subsequently, the induced folding of the flexible C-terminal tail of CP12 in the active site of GAPDH stabilizes the binary complex. Formation of several hydrogen bonds compensates the entropic cost of CP12 fixation and terminates the interaction mechanism that contributes to carbon assimilation control.

PubMed: 22514274
DOI: 10.1074/jbc.M112.350355

実験手法

X-RAY DIFFRACTION (2 Å)