Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Cryo-EM structure and molecular mechanism of the jasmonic acid transporter ABCG16.
Journal, issue, pages	Nat Plants, Vol. 10, Issue 12, Page 2052-2061, Year 2024
Publish date	Nov 4, 2024
Authors	Ning An / Xiaowei Huang / Zhao Yang / Minhua Zhang / Miaolian Ma / Fang Yu / Lianyan Jing / Boya Du / Yong-Fei Wang / Xue Zhang / Peng Zhang /
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 ...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.
External links	Nat Plants / PubMed:39496849
Methods	EM (single particle)
Resolution	2.38 - 3.32 Å
Structure data	37836 8wtm EMDB-37836, PDB-8wtm: Cryo-EM structure of jasmonic acid transporter ABCG16 bound to JA Method: EM (single particle) / Resolution: 2.65 Å 37837 8wtn EMDB-37837, PDB-8wtn: Cryo-EM structure of jasmonic acid transporter ABCG16 in occluded conformation Method: EM (single particle) / Resolution: 2.95 Å 37838 8wto EMDB-37838, PDB-8wto: Cryo-EM structure of jasmonic acid transporter ABCG16 in outward conformation Method: EM (single particle) / Resolution: 2.38 Å 37839 8wtp EMDB-37839, PDB-8wtp: Cryo-EM structure of jasmonic acid transporter ABCG16 Method: EM (single particle) / Resolution: 2.82 Å EMDB-37840: Cryo-EM structure of AtABCG16 Method: EM (single particle) / Resolution: 3.32 Å EMDB-39461: Cryo-EM structure of jasmonic acid transporter ABCG16 in digitonin Method: EM (single particle) / Resolution: 3.18 Å
Chemicals	ChemComp-JAA: {(1R,2R)-3-oxo-2-[(2Z)-pent-2-en-1-yl]cyclopentyl}acetic acid ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying moleculeYM ChemComp-VO4: VANADATE ION ChemComp-BEF: BERYLLIUM TRIFLUORIDE ION ChemComp-MG: Unknown entry ChemComp-HOH*: WATER
Source	arabidopsis thaliana (thale cress) Arabidopsis (plant)
Keywords	MEMBRANE PROTEIN / jasmonate / transport / cryo-EM / ABC transporter / plant hormone