9WFP

Structure of ABCC2(E1404Q) monomer in Arabidopsis thaliana in the DNP-GS bound state

Summary for 9WFP

• Entry DOI: 10.2210/pdb9wfp/pdb
• EMDB information: 65934
• Descriptor: ABC transporter C family member 2, GLUTATHIONE S-(2,4 DINITROBENZENE) (2 entities in total)
• Functional Keywords: plant detoxification effect, transporter, abcc2 protein, protein transport
• Biological source: Arabidopsis thaliana (thale cress)
• Total number of polymer chains: 1
• Total formula weight: 182783.35

Authors

Sun, L.,Liu, X.,Qiu, X.,Yang, Z.,Gao, Y. (deposition date: 2025-08-21, release date: 2025-12-24, Last modification date: 2026-07-08)

Primary citation

Qiu, X.,Yang, Z.,Gao, Y.,Sun, L.,Liu, X.
Structural insights into toxicant export mediated by ABCC2 in Arabidopsis thaliana.
Nat Commun, 16:11554-11554, 2025

PubMed Abstract: Plants are highly vulnerable to damage from environmental pollutants, making detoxification mechanisms essential for sustaining growth and development. ABCC2 in Arabidopsis thaliana (AtABCC2) plays a critical role in detoxification by exporting diverse toxic compounds. Here, we report the structures of AtABCC2 in three distinct states: substrate-free, bound to the substrate S-(2,4-dinitrophenyl)glutathione (DNP-GS), and bound to ATP. Both monomeric and dimeric forms of AtABCC2 are observed. Unlike other dimeric ABCC homologs, AtABCC2 features a dimer interface mediated by its transmembrane domains. DNP-GS occupies an amphipathic cavity formed by the transmembrane domains. ATP binding drives the conformational changes in each protomer which bring the transmembrane and nucleotide-binding domains closer together, transitioning the transporter from a cytosolic-facing to an occluded state. Together, these findings advance our understanding of the molecular basis of substrate binding and transport by AtABCC2, and shed light on plant detoxification mechanisms.

PubMed: 41430060
DOI: 10.1038/s41467-025-67713-5

Experimental method

ELECTRON MICROSCOPY (4.1 Å)