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Cryo-EM structures of Oryza sativa MRP5 reveal a phytate accumulation mechanism in plant vacuoles
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陈
熊
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DOI：10.1093/plcell/koag088.png)
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Abstract
En 中文
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 molecules into vacuoles, providing a molecular framework for targeted manipulation of this agriculturally important transporter. Mechanistic studies visualize how rice transports phosphate-packed phytate into storage vacuoles, enabling future crops to simultaneously reduce fertilizer pollution while preserving nutrition.
Keywords:
PHYTIC ACID ACCUMULATION
INOSITOL HEXAKISPHOSPHATE
SOFTWARE NEWS
TRANSPORTER
RESISTANCE
BINDING
GROWTH
PROTEINS
BIOSYNTHESIS
VALIDATION
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6.3W
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