7Y9V

Structure of the auxin exporter PIN1 in Arabidopsis thaliana in the IAA-bound state

Summary for 7Y9V

• Entry DOI: 10.2210/pdb7y9v/pdb
• EMDB information: 33693
• Descriptor: Auxin efflux carrier component 1, nanobody, 1H-INDOL-3-YLACETIC ACID, ... (4 entities in total)
• Functional Keywords: transport protein
• Biological source: Arabidopsis thaliana (thale cress); More
• Total number of polymer chains: 4
• Total formula weight: 161251.75

Authors

Sun, L.,Liu, X.,Yang, Z.,Xia, J. (deposition date: 2022-06-26, release date: 2022-09-07, Last modification date: 2024-11-13)

Primary citation

Yang, Z.,Xia, J.,Hong, J.,Zhang, C.,Wei, H.,Ying, W.,Sun, C.,Sun, L.,Mao, Y.,Gao, Y.,Tan, S.,Friml, J.,Li, D.,Liu, X.,Sun, L.
Structural insights into auxin recognition and efflux by Arabidopsis PIN1.
Nature, 609:611-615, 2022

PubMed Abstract: Polar auxin transport is unique to plants and coordinates their growth and development. The PIN-FORMED (PIN) auxin transporters exhibit highly asymmetrical localizations at the plasma membrane and drive polar auxin transport; 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. 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.

PubMed: 35917925
DOI: 10.1038/s41586-022-05143-9

Experimental method

ELECTRON MICROSCOPY (3.2 Å)