7Y9T

Structure of the auxin exporter PIN1 in Arabidopsis thaliana in the apo state

7Y9T の概要

• エントリーDOI: 10.2210/pdb7y9t/pdb
• EMDBエントリー: 33691
• 分子名称: Auxin efflux carrier component 1, nanobody (2 entities in total)
• 機能のキーワード: transport protein
• 由来する生物種: Arabidopsis thaliana (thale cress); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 160901.38

構造登録者

Sun, L.,Liu, X.,Yang, Z.,Xia, J. (登録日: 2022-06-26, 公開日: 2022-09-07, 最終更新日: 2024-10-30)

主引用文献

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

実験手法

ELECTRON MICROSCOPY (3.1 Å)