8iwn

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ABCG25 EQ mutant in ATP-bound state

Structural highlights

8iwn is a 2 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Electron Microscopy, Resolution 3Å
Ligands:ATP, MG
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

AB25G_ARATH High affinity abscisic acid (ABA) transporter that mediates the export of ABA, with a preference for (+)-ABA, through the plasma membrane, especially in vascular tissues (e.g. phloem companion cells), and is involved in the intercellular ABA signaling pathway (PubMed:20133881, PubMed:20935463, PubMed:24521878, PubMed:26517905). Together with ABCG31, export ABA from the endosperm to deliver it to the embryo via ABCG30 and ABCG40-mediated import to suppress radicle extension and subsequent embryonic growth (PubMed:26334616).[1] [2] [3] [4] [5]

Publication Abstract from PubMed

Abscisic acid (ABA) is a phytohormone essential to the regulation of numerous aspects of plant growth and development. The cellular level of ABA is critical to its signalling and is determined by its rate of biosynthesis, catabolism and the rates of ABA transport. ABCG25 in Arabidopsis thaliana has been identified to be an ABA exporter and play roles in regulating stomatal closure and seed germination. However, its ABA transport mechanism remains unknown. Here we report the structures of ABCG25 under different states using cryo-electron microscopy single particle analysis: the apo state and ABA-bound state of the wild-type ABCG25 and the ATP-bound state of the ATPase catalytic mutant. ABCG25 forms a homodimer. ABA binds to a cone-shaped, cytosolic-facing cavity formed in the middle of the transmembrane domains. Key residues in ABA binding are identified and verified by a cell-based ABA transport assay. ATP binding leads to closing of the nucleotide-binding domains of opposing monomers and conformational transitions of the transmembrane domains. Together, these results provide insights into the substrate recognition and transport mechanisms of ABCG25 in Arabidopsis, and facilitate our understanding of the ABA transport and signalling pathway in plants.

Structural basis for abscisic acid efflux mediated by ABCG25 in Arabidopsis thaliana.,Ying W, Liao L, Wei H, Gao Y, Liu X, Sun L Nat Plants. 2023 Oct;9(10):1697-1708. doi: 10.1038/s41477-023-01510-0. Epub 2023 , Sep 4. PMID:37666962[6]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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Citations
1 reviews cite this structure
Research Progress in the Regulation of the ABA Signaling Pathway by E3 Ubiquitin Ligases in Plants.
Kou et al. (2024)
0 more
3 other articles
No citations found

References

  1. ↑ Kuromori T, Miyaji T, Yabuuchi H, Shimizu H, Sugimoto E, Kamiya A, Moriyama Y, Shinozaki K. ABC transporter AtABCG25 is involved in abscisic acid transport and responses. Proc Natl Acad Sci U S A. 2010 Feb 2;107(5):2361-6. PMID:20133881 doi:10.1073/pnas.0912516107
  2. ↑ Kuromori T, Sugimoto E, Shinozaki K. Intertissue signal transfer of abscisic acid from vascular cells to guard cells. Plant Physiol. 2014 Apr;164(4):1587-92. PMID:24521878 doi:10.1104/pp.114.235556
  3. ↑ Kang J, Yim S, Choi H, Kim A, Lee KP, Lopez-Molina L, Martinoia E, Lee Y. Abscisic acid transporters cooperate to control seed germination. Nat Commun. 2015 Sep 3;6:8113. PMID:26334616 doi:10.1038/ncomms9113
  4. ↑ Kuromori T, Shinozaki K. ABA transport factors found in Arabidopsis ABC transporters. Plant Signal Behav. 2010 Sep;5(9):1124-6. PMID:20935463 doi:10.4161/psb.5.9.12566
  5. ↑ Borghi L, Kang J, Ko D, Lee Y, Martinoia E. The role of ABCG-type ABC transporters in phytohormone transport. Biochem Soc Trans. 2015 Oct;43(5):924-30. PMID:26517905 doi:10.1042/BST20150106
  6. ↑ Ying W, Liao L, Wei H, Gao Y, Liu X, Sun L. Structural basis for abscisic acid efflux mediated by ABCG25 in Arabidopsis thaliana. Nat Plants. 2023 Oct;9(10):1697-1708. PMID:37666962 doi:10.1038/s41477-023-01510-0

Contents


PDB ID 8iwn

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OCA

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