8WOO

Structure of the wild-type Arabidopsis ABCB19 in the brassinolide and AMP-PNP bound state

Summary for 8WOO

• Entry DOI: 10.2210/pdb8woo/pdb
• EMDB information: 37694
• Descriptor: ABC transporter B family member 19, MAGNESIUM ION, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ... (4 entities in total)
• Functional Keywords: abc transporter, transport protein
• Biological source: Arabidopsis thaliana (thale cress)
• Total number of polymer chains: 1
• Total formula weight: 138474.24

Authors

Ying, W.,Wei, H.,Liu, X.,Sun, L. (deposition date: 2023-10-07, release date: 2024-03-13, Last modification date: 2024-04-03)

Primary citation

Ying, W.,Wang, Y.,Wei, H.,Luo, Y.,Ma, Q.,Zhu, H.,Janssens, H.,Vukasinovic, N.,Kvasnica, M.,Winne, J.M.,Gao, Y.,Tan, S.,Friml, J.,Liu, X.,Russinova, E.,Sun, L.
Structure and function of the Arabidopsis ABC transporter ABCB19 in brassinosteroid export.
Science, 383:eadj4591-eadj4591, 2024

PubMed Abstract: Brassinosteroids are steroidal phytohormones that regulate plant development and physiology, including adaptation to environmental stresses. Brassinosteroids are synthesized in the cell interior but bind receptors at the cell surface, necessitating a yet to be identified export mechanism. Here, we show that a member of the ATP-binding cassette (ABC) transporter superfamily, ABCB19, functions as a brassinosteroid exporter. We present its structure in both the substrate-unbound and the brassinosteroid-bound states. Bioactive brassinosteroids are potent activators of ABCB19 ATP hydrolysis activity, and transport assays showed that ABCB19 transports brassinosteroids. In , ABCB19 and its close homolog, ABCB1, positively regulate brassinosteroid responses. Our results uncover an elusive export mechanism for bioactive brassinosteroids that is tightly coordinated with brassinosteroid signaling.

PubMed: 38513023
DOI: 10.1126/science.adj4591

Experimental method

ELECTRON MICROSCOPY (3.9 Å)