- EMDB-60369: Structure of the wild-type Arabidopsis ABCB1 in the brassinolide-... -
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Entry
Database: EMDB / ID: EMD-60369
Title
Structure of the wild-type Arabidopsis ABCB1 in the brassinolide-bound state
Map data
Sample
Complex: Purified wild-type ABCB1 protein in complex with brassinolide
Protein or peptide: ABC transporter B family member 1
Ligand: Brassinolide
Keywords
ABC transporter / wild-type / brassinolide-bound state / TRANSPORT PROTEIN
Function / homology
Function and homology information
auxin influx transmembrane transporter activity / anthocyanin accumulation in tissues in response to UV light / response to red or far red light / auxin export across the plasma membrane / stamen development / positive gravitropism / auxin efflux transmembrane transporter activity / auxin polar transport / response to blue light / photomorphogenesis ...auxin influx transmembrane transporter activity / anthocyanin accumulation in tissues in response to UV light / response to red or far red light / auxin export across the plasma membrane / stamen development / positive gravitropism / auxin efflux transmembrane transporter activity / auxin polar transport / response to blue light / photomorphogenesis / response to auxin / auxin-activated signaling pathway / plasmodesma / response to nematode / regulation of cell size / ATPase-coupled transmembrane transporter activity / ABC-type transporter activity / endoplasmic reticulum / ATP hydrolysis activity / ATP binding / plasma membrane Similarity search - Function
Type 1 protein exporter / ABC transporter transmembrane region / ABC transporter type 1, transmembrane domain / ABC transporter integral membrane type-1 fused domain profile. / ABC transporter type 1, transmembrane domain superfamily / ABC transporter-like, conserved site / ABC transporters family signature. / ABC transporter / ABC transporter-like, ATP-binding domain / ATP-binding cassette, ABC transporter-type domain profile. ...Type 1 protein exporter / ABC transporter transmembrane region / ABC transporter type 1, transmembrane domain / ABC transporter integral membrane type-1 fused domain profile. / ABC transporter type 1, transmembrane domain superfamily / ABC transporter-like, conserved site / ABC transporters family signature. / ABC transporter / ABC transporter-like, ATP-binding domain / ATP-binding cassette, ABC transporter-type domain profile. / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / P-loop containing nucleoside triphosphate hydrolase Similarity search - Domain/homology
National Natural Science Foundation of China (NSFC)
32321001; 31900885; 32322041
China
Citation
Journal: Plant Commun / Year: 2025 Title: Structural insights into brassinosteroid export mediated by the Arabidopsis ABC transporter ABCB1. Authors: Hong Wei / Heyuan Zhu / Wei Ying / Hilde Janssens / Miroslav Kvasnica / Johan M Winne / Yongxiang Gao / Jiří Friml / Qian Ma / Shutang Tan / Xin Liu / Eugenia Russinova / Linfeng Sun / Abstract: Brassinosteroids (BRs) are steroidal phytohormones indispensable for plant growth, development, and responses to environmental stresses. The export of bioactive BRs to the apoplast is essential for ...Brassinosteroids (BRs) are steroidal phytohormones indispensable for plant growth, development, and responses to environmental stresses. The export of bioactive BRs to the apoplast is essential for BR signaling initiation, which requires binding of a BR molecule to the extracellular domains of the plasma membrane-localized receptor complex. We have previously shown that the Arabidopsis thaliana ATP-binding cassette (ABC) transporter ABCB19 functions as a BR exporter and, together with its close homolog ABCB1, positively regulates BR signaling. Here, we demonstrate that ABCB1 is another BR transporter. The ATP hydrolysis activity of ABCB1 can be stimulated by bioactive BRs, and its transport activity was confirmed in proteoliposomes and protoplasts. Structures of ABCB1 were determined in substrate-unbound (apo), brassinolide (BL)-bound, and ATP plus BL-bound states. In the BL-bound structure, BL is bound to the hydrophobic cavity formed by the transmembrane domain and triggers local conformational changes. Together, our data provide additional insights into ABC transporter-mediated BR export.
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