EMDB/PDB/SASBDBから引用されている文献のデータベース

キーワード
構造解析手法	All X線回折 NMR 電子顕微鏡小角散乱中性子線回折線維回折粉末回折赤外分光 EPR FRET 理論モデルハイブリッド
著者・登録者
ジャーナル
IF	>30 >20 >10 >5 all

タイトル	The plastidial PHS1-DPE1 complex drives efficient malto-oligosaccharides synthesis in rice starch metabolism.
ジャーナル・号・ページ	Nat Commun, Vol. 17, Issue 1, Year 2026
掲載日	2026年5月3日
著者	Jian Liu / Xinru Wu / Haitao He / Xi Yang / Yuanhuai Hu / Fei Zhang / Rong Fan / Xuecui Wang / Shenao Yang / Lian Xiong / Delin Zhang / Ping Yin / Jianping Guo / Zhu Liu / Junjie Yan /
PubMed 要旨	Starch serves as a vital energy reserve in plants. During its biosynthesis, malto-oligosaccharides (MOS) are essential primers. One of the key pathways for MOS production involves plastidial α- ...Starch serves as a vital energy reserve in plants. During its biosynthesis, malto-oligosaccharides (MOS) are essential primers. One of the key pathways for MOS production involves plastidial α-glucan phosphorylase (PHS1/Pho1) and disproportionating enzyme (DPE1). However, the functional relationship between these enzymes is unclear. Here, we demonstrate that rice PHS1 and DPE1 assemble into a multimeric complex. Cryo-EM structures of the PHS1-DPE1 complex reveal an assembly mechanism and suggest a potential substrate tunnel. Biochemical assays show the complex dramatically enhances catalytic efficiency over individual enzymes. Single-molecule fluorescence resonance energy transfer (smFRET) visualizes conformational dynamics, enabling rapid substrate transfer between the enzymes. We further identify the unique L80 loop in PHS1 as a potential regulator. Its deletion reduces catalytic efficiency and prolongs conformational state lifetimes during substrate transfer, thereby reducing the production of longer MOSs. Our findings establish that the PHS1-DPE1 complex facilitates efficient MOS primer synthesis through efficient substrate transfer or diffusion between the two enzymes, providing mechanistic insight into a critical step of starch biosynthesis with agronomic implications.
リンク	Nat Commun / PubMed:42069819 / PubMed Central
手法	EM (単粒子)
解像度	2.4 - 3.07 Å
構造データ	63277 9lpw EMDB-63277, PDB-9lpw: Cryo-EM structure of rice PHS1-DPE1 complex 手法: EM (単粒子) / 解像度: 2.78 Å EMDB-63278: Cryo-EM structure of rice PHS1-DPE1 complex 手法: EM (単粒子) / 解像度: 2.78 Å EMDB-63279: Cryo-EM structure of rice DPE1 dimer 手法: EM (単粒子) / 解像度: 2.86 Å EMDB-63280: Cryo-EM structure of rice PHS1 dimer 手法: EM (単粒子) / 解像度: 2.61 Å 63281 9lpz EMDB-63281, PDB-9lpz: Cryo-EM structure of rice PHS1-DPE1 complex 手法: EM (単粒子) / 解像度: 2.4 Å EMDB-63686: cryo-EM structure of a catalytic inactive mutant(R709A) of PHS1 dimer 手法: EM (単粒子) / 解像度: 2.96 Å EMDB-63687: cryo-EM structure of a catalytic inactive mutant(D391A) of DPE1 dimer 手法: EM (単粒子) / 解像度: 3.03 Å EMDB-63688: cryo-EM structure of maltose and glucose bound rice PHS1(R709A)-DPE1(D391A) complex 手法: EM (単粒子) / 解像度: 3.02 Å 63699 9m80 EMDB-63699, PDB-9m80: cryo-EM structure of maltose and glucose bound rice PHS1(R709A)-DPE1(D391A) complex 手法: EM (単粒子) / 解像度: 3.07 Å
化合物	ChemComp-GLC: alpha-D-glucopyranose
由来	Oryza sativa subsp. japonica (Rice) (イネ) oryza sativa japonica group (イネ)
キーワード	TRANSFERASE / Complex / Starch biosynthersis / Rice / Maltooligosaccharide elongation / inactive mutant