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	Structural insights into AtABCG25, an angiosperm-specific abscisic acid exporter.
Journal, issue, pages	Plant Commun, Vol. 5, Issue 1, Page 100776, Year 2024
Publish date	Jan 8, 2024
Authors	Jian Xin / Yeling Zhou / Yichun Qiu / He Geng / Yuzhu Wang / Yi Song / Jiansheng Liang / Kaige Yan /
PubMed Abstract	Cellular hormone homeostasis is essential for precise spatial and temporal signaling responses and plant fitness. Abscisic acid (ABA) plays pivotal roles in orchestrating various developmental and ...Cellular hormone homeostasis is essential for precise spatial and temporal signaling responses and plant fitness. Abscisic acid (ABA) plays pivotal roles in orchestrating various developmental and stress responses and confers fitness benefits over ecological and evolutionary timescales in terrestrial plants. Cellular ABA level is regulated by complex processes, including biosynthesis, catabolism, and transport. AtABCG25 is the first ABA exporter identified through genetic screening and affects diverse ABA responses. Resolving the structural basis of ABA export by ABCG25 is critical for further manipulations of ABA homeostasis and plant fitness. We used cryo-electron microscopy to elucidate the structural dynamics of AtABCG25 and successfully characterized different states, including apo AtABCG25, ABA-bound AtABCG25, and ATP-bound AtABCG25 (E232Q). Notably, AtABCG25 forms a homodimer that features a deep, slit-like cavity in the transmembrane domain, and we precisely characterized the critical residues in the cavity where ABA binds. ATP binding triggers closure of the nucleotide-binding domains and conformational transitions in the transmembrane domains. We show that AtABCG25 belongs to a conserved ABCG subfamily that originated during the evolution of angiosperms. This subfamily neofunctionalized to regulate seed germination via the endosperm, in concert with the evolution of this angiosperm-specific, embryo-nourishing tissue. Collectively, these findings provide valuable insights into the intricate substrate recognition and transport mechanisms of the ABA exporter AtABCG25, paving the way for genetic manipulation of ABA homeostasis and plant fitness.
External links	Plant Commun / PubMed:38050355 / PubMed Central
Methods	EM (single particle)
Resolution	2.87 - 3.23 Å
Structure data	37397 8wam EMDB-37397, PDB-8wam: Cryo-EM structure of the ABCG25 E232Q mutant bound to ATP and Magnesium Method: EM (single particle) / Resolution: 3.23 Å 37418 8wba EMDB-37418, PDB-8wba: Cryo-EM structure of the ABCG25 bound to CHS Method: EM (single particle) / Resolution: 3.1 Å 37426 8wbx EMDB-37426, PDB-8wbx: Cryo-EM structure of the ABCG25 bound to ABA Method: EM (single particle) / Resolution: 3.23 Å 37455 8wd6 EMDB-37455, PDB-8wd6: Cryo-EM structure of the ABCG25 Method: EM (single particle) / Resolution: 2.87 Å
Chemicals	ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying moleculeYM / Adenosine triphosphate ChemComp-MG: Unknown entry ChemComp-Y01: CHOLESTEROL HEMISUCCINATE 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 / Abscisic acid
Source	Arabidopsis arenosa (plant) arabidopsis thaliana (thale cress)
Keywords	TRANSPORT PROTEIN / exporter / complex / transporter / MEMBRANE PROTEIN