8WTM

Cryo-EM structure of jasmonic acid transporter ABCG16 bound to JA

8WTM の概要

• エントリーDOI: 10.2210/pdb8wtm/pdb
• EMDBエントリー: 37836
• 分子名称: ABC transporter G family member 16, {(1R,2R)-3-oxo-2-[(2Z)-pent-2-en-1-yl]cyclopentyl}acetic acid (2 entities in total)
• 機能のキーワード: jasmonate, transport, cryo-em, abc transporter, plant hormone, 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: 164005.40

構造登録者

Huang, X.,An, N.,Zhang, X.,Zhang, P. (登録日: 2023-10-19, 公開日: 2024-10-23, 最終更新日: 2025-01-01)

主引用文献

An, N.,Huang, X.,Yang, Z.,Zhang, M.,Ma, M.,Yu, F.,Jing, L.,Du, B.,Wang, Y.F.,Zhang, X.,Zhang, P.
Cryo-EM structure and molecular mechanism of the jasmonic acid transporter ABCG16.
Nat.Plants, 10:2052-2061, 2024

PubMed Abstract: Jasmonates (JAs) are a class of oxylipin phytohormones including jasmonic acid (JA) and derivatives that regulate plant growth, development and biotic and abiotic stress. A number of transporters have been identified to be responsible for the cellular and subcellular translocation of JAs. However, the mechanistic understanding of how these transporters specifically recognize and transport JAs is scarce. Here we determined the cryogenic electron microscopy structure of JA exporter AtABCG16 in inward-facing apo, JA-bound and occluded conformations, and outward-facing post translocation conformation. AtABCG16 structure forms a homodimer, and each monomer contains a nucleotide-binding domain, a transmembrane domain and an extracellular domain. Structural analyses together with biochemical and plant physiological experiments revealed the molecular mechanism by which AtABCG16 specifically recognizes and transports JA. Structural analyses also revealed that AtABCG16 features a unique bifurcated substrate translocation pathway, which is composed of two independent substrate entrances, two substrate-binding pockets and a shared apoplastic cavity. In addition, residue Phe608 from each monomer is disclosed to function as a gate along the translocation pathway controlling the accessing of substrate JA from the cytoplasm or apoplast. Based on the structural and biochemical analyses, a working model of AtABCG16-mediated JA transport is proposed, which diversifies the molecular mechanisms of ABC transporters.

PubMed: 39496849
DOI: 10.1038/s41477-024-01839-0

実験手法

ELECTRON MICROSCOPY (2.65 Å)