Structural highlights
Function
[ATM1_YEAST] Performs an essential function in the generation of cytoplasmic iron-sulfur proteins by mediating export of Fe/S cluster precursors synthesized by NFS1 and other mitochondrial proteins.[1]
Publication Abstract from PubMed
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.
Crystal structures of nucleotide-free and glutathione-bound mitochondrial ABC transporter Atm1.,Srinivasan V, Pierik AJ, Lill R Science. 2014 Mar 7;343(6175):1137-40. doi: 10.1126/science.1246729. PMID:24604199[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kispal G, Csere P, Prohl C, Lill R. The mitochondrial proteins Atm1p and Nfs1p are essential for biogenesis of cytosolic Fe/S proteins. EMBO J. 1999 Jul 15;18(14):3981-9. PMID:10406803 doi:http://dx.doi.org/10.1093/emboj/18.14.3981
- ↑ Srinivasan V, Pierik AJ, Lill R. Crystal structures of nucleotide-free and glutathione-bound mitochondrial ABC transporter Atm1. Science. 2014 Mar 7;343(6175):1137-40. doi: 10.1126/science.1246729. PMID:24604199 doi:http://dx.doi.org/10.1126/science.1246729
