- EMDB-37690: Structure of the wild-type Arabidopsis ABCB19 in the apo state -
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Entry
Database: EMDB / ID: EMD-37690
Title
Structure of the wild-type Arabidopsis ABCB19 in the apo state
Map data
Sample
Organelle or cellular component: Purified wild-type ABCB19 protein
Protein or peptide: ABC transporter B family member 19
Keywords
ABC transporter / wild-type / apo state / TRANSPORT PROTEIN
Function / homology
Function and homology information
acropetal auxin transport / anthocyanin accumulation in tissues in response to UV light / response to red or far red light / formation of plant organ boundary / basipetal auxin transport / auxin transport / positive gravitropism / stamen development / auxin efflux transmembrane transporter activity / auxin polar transport ...acropetal auxin transport / anthocyanin accumulation in tissues in response to UV light / response to red or far red light / formation of plant organ boundary / basipetal auxin transport / auxin transport / positive gravitropism / stamen development / auxin efflux transmembrane transporter activity / auxin polar transport / lateral root development / response to far red light / photomorphogenesis / response to blue light / root development / response to auxin / auxin-activated signaling pathway / regulation of cell size / ABC-type transporter activity / ATP hydrolysis activity / ATP binding / plasma membrane / cytosol 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)
31900885; 31870732; 32322041
China
Citation
Journal: Science / Year: 2024 Title: Structure and function of the ABC transporter ABCB19 in brassinosteroid export. Authors: Wei Ying / Yaowei Wang / Hong Wei / Yongming Luo / Qian Ma / Heyuan Zhu / Hilde Janssens / Nemanja Vukašinović / Miroslav Kvasnica / Johan M Winne / Yongxiang Gao / Shutang Tan / Jiří ...Authors: Wei Ying / Yaowei Wang / Hong Wei / Yongming Luo / Qian Ma / Heyuan Zhu / Hilde Janssens / Nemanja Vukašinović / Miroslav Kvasnica / Johan M Winne / Yongxiang Gao / Shutang Tan / Jiří Friml / Xin Liu / Eugenia Russinova / Linfeng Sun / Abstract: Brassinosteroids are steroidal phytohormones that regulate plant development and physiology, including adaptation to environmental stresses. Brassinosteroids are synthesized in the cell interior but ...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.
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