Structural insights into auxin recognition and efflux by Arabidopsis PIN1

Article

关键词: CRYSTAL-STRUCTURE;    TRANSPORT;    MECHANISM;    PROTEIN;    ACID;    HOMEOSTASIS;    ANTIPORTER;   

DOI  :  10.1038/s41586-022-05143-9

来源: SCIE

【 摘 要 】

Polar auxin transport is unique to plants and coordinates their growth and development(1,2). The PIN-FORMED (PIN) auxin transporters exhibit highly asymmetrical localizations at the plasma membrane and drive polar auxin transport(3,4); however, their structures and transport mechanisms remain largely unknown. Here, we report three inward-facing conformation structures of Arabidopsis thaliana PIN1: the apo state, bound to the natural auxin indole-3-acetic acid (IAA), and in complex with the polar auxin transport inhibitor N-1-naphthylphthalamic acid (NPA). The transmembrane domain of PIN1 shares a conserved NhaA fold(5). In the substrate-bound structure, IAA is coordinated by both hydrophobic stacking and hydrogen bonding. NPA competes with IAA for the same site at the intracellular pocket, but with a much higher affinity. These findings inform our understanding of the substrate recognition and transport mechanisms of PINs and set up a framework for future research on directional auxin transport, one of the most crucial processes underlying plant development.

【 授权许可】

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