7QPC

Inward-facing NPA bound form of auxin transporter PIN8

7QPC の概要

• エントリーDOI: 10.2210/pdb7qpc/pdb
• 関連するPDBエントリー: 7QP9 7QPA
• EMDBエントリー: 14117 14118
• 分子名称: Auxin efflux carrier component 8, 2-(naphthalen-1-ylcarbamoyl)benzoic acid, 1,2-DILINOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE, ... (4 entities in total)
• 機能のキーワード: auxin transport, aec family, bart superfamily, membrane protein
• 由来する生物種: Arabidopsis thaliana (thale cress)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 85228.84

構造登録者

Ung, K.L.,Winkler, M.B.L.,Dedic, E.,Stokes, D.L.,Pedersen, B.P. (登録日: 2022-01-03, 公開日: 2022-07-06, 最終更新日: 2024-11-13)

主引用文献

Ung, K.L.,Winkler, M.,Schulz, L.,Kolb, M.,Janacek, D.P.,Dedic, E.,Stokes, D.L.,Hammes, U.Z.,Pedersen, B.P.
Structures and mechanism of the plant PIN-FORMED auxin transporter.
Nature, 609:605-610, 2022

PubMed Abstract: Auxins are hormones that have central roles and control nearly all aspects of growth and development in plants. The proteins in the PIN-FORMED (PIN) family (also known as the auxin efflux carrier family) are key participants in this process and control auxin export from the cytosol to the extracellular space. Owing to a lack of structural and biochemical data, the molecular mechanism of PIN-mediated auxin transport is not understood. Here we present biophysical analysis together with three structures of Arabidopsis thaliana PIN8: two outward-facing conformations with and without auxin, and one inward-facing conformation bound to the herbicide naphthylphthalamic acid. The structure forms a homodimer, with each monomer divided into a transport and scaffold domain with a clearly defined auxin binding site. Next to the binding site, a proline-proline crossover is a pivot point for structural changes associated with transport, which we show to be independent of proton and ion gradients and probably driven by the negative charge of the auxin. The structures and biochemical data reveal an elevator-type transport mechanism reminiscent of bile acid/sodium symporters, bicarbonate/sodium symporters and sodium/proton antiporters. Our results provide a comprehensive molecular model for auxin recognition and transport by PINs, link and expand on a well-known conceptual framework for transport, and explain a central mechanism of polar auxin transport, a core feature of plant physiology, growth and development.

PubMed: 35768502
DOI: 10.1038/s41586-022-04883-y

実験手法

ELECTRON MICROSCOPY (3.44 Å)