Journal
SCIENCE
Volume 343, Issue 6175, Pages 1137-1140Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1246729
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Funding
- Deutsche Forschungsgemeinschaft [SFB 593, SFB 987, GRK 1216]
- von Behring-Rontgen Stiftung
- LOEWE program of state Hessen
- Max-Planck Gesellschaft
- Feldberg Foundation
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The yeast mitochondrial ABC transporter Atm1, in concert with glutathione, functions in the export of a substrate required for cytosolic-nuclear iron-sulfur protein biogenesis and cellular iron regulation. Defects in the human ortholog ABCB7 cause the sideroblastic anemia XLSA/A. Here, we report the crystal structures of free and glutathione-bound Atm1 in inward-facing, open conformations at 3.06- and 3.38-angstrom resolution, respectively. The glutathione binding site includes a residue mutated in XLSA/A and is located close to the inner membrane surface in a large cavity. The two nucleotide-free adenosine 5'-triphosphate binding domains do not interact yet are kept in close vicinity through tight interaction of the two C-terminal alpha-helices of the Atm1 dimer. The resulting protein stabilization may be a common structural feature of all ABC exporters.
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