EMD-37839

Single-particle
2.82 Å
EMD-37839 Deposition: 19/10/2023
Map released: 23/10/2024
Last modified: 01/01/2025
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-37839

Cryo-EM structure of jasmonic acid transporter ABCG16

EMD-37839

Single-particle
2.82 Å
EMD-37839 Deposition: 19/10/2023
Map released: 23/10/2024
Last modified: 01/01/2025
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Arabidopsis thaliana
Sample: Homodimer of ABCG16
Fitted models: 8wtp (Avg. Q-score: 0.545)

Deposition Authors: Huang X , An N , Zhang X , Zhang P
Cryo-EM structure and molecular mechanism of the jasmonic acid transporter ABCG16.
An N , Huang X , Yang Z , Zhang M, Ma M, Yu F, Jing L, Du B , Wang YF, Zhang X , Zhang P
(2024) Nat Plants , 10 , 2052 - 2061
PUBMED: 39496849
DOI: doi:10.1038/s41477-024-01839-0
ISSN: 2055-0278
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.