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TitleGlutathione binding to the plant Atm3 transporter and implications for the conformational coupling of ABC transporters.
Journal, issue, pagesElife, Vol. 11, Year 2022
Publish dateMar 25, 2022
AuthorsChengcheng Fan / Douglas C Rees /
PubMed AbstractThe ATP binding cassette (ABC) transporter of mitochondria (Atm) from (Atm3) has been implicated in the maturation of cytosolic iron-sulfur proteins and heavy metal detoxification, plausibly by ...The ATP binding cassette (ABC) transporter of mitochondria (Atm) from (Atm3) 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 Atm3 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-VO. 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 inhibitory mixed disulfides with GSSG. Despite extensive efforts, we were unable to prepare the ternary complex of Atm3 containing both GSSG and MgATP. A survey of structurally characterized type IV ABC transporters that includes Atm3 establishes that while nucleotides are found associated with all conformational states, they are effectively required to stabilize occluded, closed, and outward-facing conformations. In contrast, transport substrates have only been observed associated with inward-facing conformations. The absence of structures with dimerized nucleotide binding domains containing both nucleotide and transport substrate suggests that this form of the ternary complex exists only transiently during the transport cycle.
External linksElife / PubMed:35333177 / PubMed Central
MethodsEM (single particle)
Resolution3.4 - 3.95 Å
Structure data

24182

7n58

EMDB-24182, PDB-7n58:
Structure of AtAtm3 in the inward-facing conformation
Method: EM (single particle) / Resolution: 3.4 Å

24183

7n59

EMDB-24183, PDB-7n59:
Structure of AtAtm3 in the inward-facing conformation with GSSG bound
Method: EM (single particle) / Resolution: 3.6 Å

24184

7n5a

EMDB-24184, PDB-7n5a:
Structure of AtAtm3 in the closed conformation
Method: EM (single particle) / Resolution: 3.95 Å

24185

7n5b

EMDB-24185, PDB-7n5b:
Structure of AtAtm3 in the outward-facing conformation
Method: EM (single particle) / Resolution: 3.8 Å

Chemicals

ChemComp-GDS:
OXIDIZED GLUTATHIONE DISULFIDE

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

ChemComp-VO4:
VANADATE ION

ChemComp-MG:
Unknown entry

Source
  • arabidopsis thaliana (thale cress)
KeywordsMEMBRANE PROTEIN / ABC transporter / ATPase

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