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TitleCryo-EM structures of Oryza sativa MRP5 reveal a phytate accumulation mechanism in plant vacuoles.
Journal, issue, pagesPlant Cell, Year 2026
Publish dateMar 24, 2026
AuthorsJiaqi Zuo / Jie Zhang / Ying Tang / Lihuan Jiang / Shuo Cao / Yan Liu / Cuicui Shen / Chuang Wang / Hao Chen / Lizhong Xiong / Ping Yin / Zhou Gong / Zhu Liu /
PubMed AbstractPhytate (phytic acid, or InsP6), the primary phosphorus storage compound in plants, plays essential roles in nutrient homeostasis and cellular signaling. However, its strong metal-chelating ...Phytate (phytic acid, or InsP6), the primary phosphorus storage compound in plants, plays essential roles in nutrient homeostasis and cellular signaling. However, its strong metal-chelating properties make cytosolic accumulation cytotoxic, necessitating its sequestration into vacuoles for safe storage. Here, we present the cryo-EM structures of the rice vacuolar phytate transporter, OsMRP5, captured in distinct functional states. These structures reveal the molecular basis of OsMRP5 function as an ATP-binding cassette (ABC) transporter. OsMRP5 employs a specialized substrate-recognition mechanism, uniquely adapted to bind the fully hydrophilic InsP6 through extensive electrostatic and hydrogen-bonding interactions within two distinct, highly polar binding sites in its central cavity. A distinctive electropositive tunnel, positioned above the central cavity, forms a continuous pathway connecting the InsP6-binding pocket to the vacuolar export site. This tunnel likely generates an electrostatic attraction that facilitates the movement of the highly anionic InsP6 through the transporter. By mapping mutations from low-phytic acid (lpa) crop variants onto the OsMRP5 structures, we pinpoint their conserved locations critical for transporter function and validate their impact experimentally. These results reveal how OsMRP5 recognizes and transports the highly charged InsP6 molecule into vacuoles, providing a molecular framework for targeted manipulation of this agriculturally important transporter.
External linksPlant Cell / PubMed:41875395
MethodsEM (single particle)
Resolution2.63 - 3.5 Å
Structure data

65282

9vrb

EMDB-65282, PDB-9vrb:
Cryo-EM structure of ATP-bound Oryza sativa MRP5 with E1424Q mutation
Method: EM (single particle) / Resolution: 2.63 Å

65283

9vrc

EMDB-65283, PDB-9vrc:
Cryo-EM structure of Oryza sativa multidrug resistance protein 5 (MRP5)
Method: EM (single particle) / Resolution: 3.21 Å

65284

9vrd

EMDB-65284, PDB-9vrd:
Cryo-EM structure of rice multidrug resistance protein 5 (MRP5) with InsP6 in state A
Method: EM (single particle) / Resolution: 3.03 Å

65285

9vre

EMDB-65285, PDB-9vre:
Cryo-EM structure of rice multidrug resistance protein 5 (MRP5) with InsP6 in state B
Method: EM (single particle) / Resolution: 3.5 Å

Chemicals

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

ChemComp-MG:
Unknown entry

ChemComp-IHP:
INOSITOL HEXAKISPHOSPHATE

Source
  • oryza sativa japonica group (Japanese rice)
KeywordsTRANSPORT PROTEIN / ABC-type transporter / Monomer

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