8WTO

Cryo-EM structure of jasmonic acid transporter ABCG16 in outward conformation

Summary for 8WTO

• Entry DOI: 10.2210/pdb8wto/pdb
• EMDB information: 37838
• Descriptor: ABC transporter G family member 16, ADENOSINE-5'-DIPHOSPHATE, BERYLLIUM TRIFLUORIDE ION, ... (5 entities in total)
• Functional Keywords: jasmonate, transport, cryo-em, abc transporter, plant hormone, membrane protein
• Biological source: Arabidopsis thaliana (thale cress)
• Total number of polymer chains: 2
• Total formula weight: 164619.89

Authors

Huang, X.,An, N.,Zhang, X.,Zhang, P. (deposition date: 2023-10-19, release date: 2024-10-23, Last modification date: 2025-01-01)

Primary citation

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

Experimental method

ELECTRON MICROSCOPY (2.38 Å)