Glutathione binding to the plant AtAtm3 transporter and implications for the conformational coupling of ABC transporters.

ABSTRACT: The ATP binding cassette (ABC) transporter of mitochondria (Atm) from Arabidopsis thaliana (AtAtm3) has been implicated in the maturation of cytosolic iron-sulfur proteins and heavy metal detoxification, plausibly by exporting glutathione derivatives. Using single-particle cryo-electron microscopy, we have determined four structures of AtAtm3 in three different conformational states: two inward-facing conformations (with and without bound oxidized glutathione [GSSG]), together with closed and outward-facing states stabilized by MgADP-VO₄. These structures not only provide a structural framework for defining the alternating access transport cycle, but also reveal the paucity of cysteine residues in the glutathione binding site that could potentially form inhi

SUBMITTER: Fan C 

PROVIDER: S-EPMC9000953 | biostudies-literature | 2022 Mar

REPOSITORIES: biostudies-literature