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TitleConformational changes in the yeast mitochondrial ABC transporter Atm1 during the transport cycle.
Journal, issue, pagesSci Adv, Vol. 7, Issue 52, Page eabk2392, Year 2021
Publish dateDec 24, 2021
AuthorsThomas L Ellinghaus / Thomas Marcellino / Vasundara Srinivasan / Roland Lill / Werner Kühlbrandt /
PubMed AbstractThe mitochondrial inner membrane ABC transporter Atm1 exports an unknown substrate to the cytosol for iron-sulfur protein biogenesis, cellular iron regulation, and tRNA thio-modification. Mutations ...The mitochondrial inner membrane ABC transporter Atm1 exports an unknown substrate to the cytosol for iron-sulfur protein biogenesis, cellular iron regulation, and tRNA thio-modification. Mutations in the human relative ABCB7 cause the iron storage disease XLSA/A. We determined 3D structures of two complementary states of Atm1 in lipid nanodiscs by electron cryo-microscopy at 2.9- to 3.4-Å resolution. The inward-open structure resembled the known crystal structure of nucleotide-free apo-Atm1 closely. The occluded conformation with bound AMP-PNP-Mg showed a tight association of the two nucleotide-binding domains, a rearrangement of the C-terminal helices, and closure of the putative substrate-binding cavity in the homodimeric transporter. We identified a hydrophobic patch on the C-terminal helices of yeast Atm1, which is unique among type IV ABC transporters of known structure. Truncation mutants of yeast Atm1 suggest that the C-terminal helices stabilize the dimer, yet are not necessary for closure of the nucleotide-binding domains.
External linksSci Adv / PubMed:34936443 / PubMed Central
MethodsEM (single particle)
Resolution2.9 - 7.1 Å
Structure data

EMDB-13613, PDB-7psl:
S. cerevisiae Atm1 in MSP1D1 nanodiscs in nucleotide-free state
Method: EM (single particle) / Resolution: 3.3 Å

EMDB-13614, PDB-7psm:
S. cerevisiae Atm1 in MSP1D1 nanodiscs with bound AMP-PNP and Mg2+
Method: EM (single particle) / Resolution: 3.4 Å

EMDB-13615, PDB-7psn:
S. cerevisiae Atm1 in MSP1E3D1 nanodiscs with bound AMP-PNP and Mg2+
Method: EM (single particle) / Resolution: 2.9 Å

EMDB-13616:
C. thermophilum Atm1 in MSP1E3D1 nanodiscs in nucleotide-free state, class 1
Method: EM (single particle) / Resolution: 7.1 Å

EMDB-13617:
C. thermophilum Atm1 in MSP1E3D1 nanodiscs in nucleotide-free state, class 2
Method: EM (single particle) / Resolution: 4.6 Å

EMDB-13618:
C. thermophilum Atm1 in MSP1E3D1 nanodiscs in nucleotide-free state, class 3
Method: EM (single particle) / Resolution: 4.2 Å

Chemicals

ChemComp-LOP:
(1R)-2-{[(R)-(2-AMINOETHOXY)(HYDROXY)PHOSPHORYL]OXY}-1-[(DODECANOYLOXY)METHYL]ETHYL (9Z)-OCTADEC-9-ENOATE / phospholipid*YM

ChemComp-PO4:
PHOSPHATE ION / Phosphate

ChemComp-ANP:
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP, energy-carrying molecule analogue*YM

ChemComp-MG:
Unknown entry

Source
  • saccharomyces cerevisiae (strain atcc 204508 / s288c) (yeast)
  • Saccharomyces cerevisiae (brewer's yeast)
  • Chaetomium thermophilum (fungus)
KeywordsTRANSPORT PROTEIN / ABC transporter

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