Structural insights into auxin recognition and efflux by Arabidopsis PIN1.

ABSTRACT: 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 fold⁵. In the substrate-bound structure, IAA is coordinated by both hydrophobic stacking and hydrogen bonding. NPA competes with IAA for the same site a

SUBMITTER: Yang Z 

PROVIDER: S-EPMC9477737 | biostudies-literature | 2022 Sep

REPOSITORIES: biostudies-literature