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 abscisic acid transporter ABCG25.
Journal, issue, pages	Nat Plants, Vol. 9, Issue 10, Page 1709-1719, Year 2023
Publish date	Sep 4, 2023
Authors	Xiaowei Huang / Xue Zhang / Ning An / Minhua Zhang / Miaolian Ma / Yang Yang / Lianyan Jing / Yongfei Wang / Zhenguo Chen / Peng Zhang /
PubMed Abstract	Abscisic acid (ABA) is one of the plant hormones that regulate various physiological processes, including stomatal closure, seed germination and development. ABA is synthesized mainly in vascular ...Abscisic acid (ABA) is one of the plant hormones that regulate various physiological processes, including stomatal closure, seed germination and development. ABA is synthesized mainly in vascular tissues and transported to distal sites to exert its physiological functions. Many ABA transporters have been identified, however, the molecular mechanism of ABA transport remains elusive. Here we report the cryogenic electron microscopy structure of the Arabidopsis thaliana adenosine triphosphate-binding cassette G subfamily ABA exporter ABCG25 (AtABCG25) in inward-facing apo conformation, ABA-bound pre-translocation conformation and outward-facing occluded conformation. Structural and biochemical analyses reveal that the ABA bound with ABCG25 adopts a similar configuration as that in ABA receptors and that the ABA-specific binding is dictated by residues from transmembrane helices TM1, TM2 and TM5a of each protomer at the transmembrane domain interface. Comparison of different conformational structures reveals conformational changes, especially those of transmembrane helices and residues constituting the substrate translocation pathway during the cross-membrane transport process. Based on the structural data, a 'gate-flipper' translocation model of ABCG25-mediated ABA cross-membrane transport is proposed. Our structural data on AtABCG25 provide new clues to the physiological study of ABA and shed light on its potential applications in plants and agriculture.
External links	Nat Plants / PubMed:37666961
Methods	EM (single particle)
Resolution	2.81 - 3.08 Å
Structure data	35145 8i38 EMDB-35145, PDB-8i38: Cryo-EM structure of abscisic acid transporter AtABCG25 in inward conformation Method: EM (single particle) / Resolution: 2.9 Å 35146 8i39 EMDB-35146, PDB-8i39: Cryo-EM structure of abscisic acid transporter AtABCG25 with ABA Method: EM (single particle) / Resolution: 2.85 Å 35147 8i3a EMDB-35147, PDB-8i3a: Cryo-EM structure of abscisic acid transporter AtABCG25 in outward conformation Method: EM (single particle) / Resolution: 3.04 Å 35148 8i3b EMDB-35148, PDB-8i3b: Cryo-EM structure of abscisic acid transporter AtABCG25 in nanodisc Method: EM (single particle) / Resolution: 3.08 Å 35149 8i3c EMDB-35149, PDB-8i3c: Cryo-EM structure of abscisic acid transporter AtABCG25 with CHS Method: EM (single particle) / Resolution: 2.85 Å 35150 8i3d EMDB-35150, PDB-8i3d: Cryo-EM structure of abscisic acid transporter AtABCG25 Method: EM (single particle) / Resolution: 2.81 Å
Chemicals	ChemComp-A8S: (2Z,4E)-5-[(1S)-1-hydroxy-2,6,6-trimethyl-4-oxocyclohex-2-en-1-yl]-3-methylpenta-2,4-dienoic acid / hormoneYM ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying moleculeYM ChemComp-MG: Unknown entry ChemComp-Y01: CHOLESTEROL HEMISUCCINATE
Source	arabidopsis thaliana (thale cress)
Keywords	MEMBRANE PROTEIN / abscisic acid / transport / ABC transporter / plant hormone