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TitleThe plastidial PHS1-DPE1 complex drives efficient malto-oligosaccharides synthesis in rice starch metabolism.
Journal, issue, pagesNat Commun, Vol. 17, Year 2026
Publish dateMar 11, 2025
AuthorsJian 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 AbstractStarch 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.
External linksNat Commun / PubMed:42069819 / PubMed Central
MethodsEM (single particle)
Resolution2.4 - 3.07 Å
Structure data

63277

9lpw

EMDB-63277, PDB-9lpw:
Cryo-EM structure of rice PHS1-DPE1 complex
Method: EM (single particle) / Resolution: 2.78 Å

EMDB-63278: Cryo-EM structure of rice PHS1-DPE1 complex
Method: EM (single particle) / Resolution: 2.78 Å

EMDB-63279: Cryo-EM structure of rice DPE1 dimer
Method: EM (single particle) / Resolution: 2.86 Å

EMDB-63280: Cryo-EM structure of rice PHS1 dimer
Method: EM (single particle) / Resolution: 2.61 Å

63281

9lpz

EMDB-63281, PDB-9lpz:
Cryo-EM structure of rice PHS1-DPE1 complex
Method: EM (single particle) / Resolution: 2.4 Å

EMDB-63686: cryo-EM structure of a catalytic inactive mutant(R709A) of PHS1 dimer
Method: EM (single particle) / Resolution: 2.96 Å

EMDB-63687: cryo-EM structure of a catalytic inactive mutant(D391A) of DPE1 dimer
Method: EM (single particle) / Resolution: 3.03 Å

EMDB-63688: cryo-EM structure of maltose and glucose bound rice PHS1(R709A)-DPE1(D391A) complex
Method: EM (single particle) / Resolution: 3.02 Å

63699

9m80

EMDB-63699, PDB-9m80:
cryo-EM structure of maltose and glucose bound rice PHS1(R709A)-DPE1(D391A) complex
Method: EM (single particle) / Resolution: 3.07 Å

Chemicals

ChemComp-GLC:
alpha-D-glucopyranose

Source
  • Oryza sativa subsp. japonica (Rice) (Japanese rice)
  • oryza sativa japonica group (Japanese rice)
KeywordsTRANSFERASE / Complex / Starch biosynthersis / Rice / Maltooligosaccharide elongation / inactive mutant

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