4myc | pdb_00004myc

Structure of the mitochondrial ABC transporter, Atm1

spinqualitylabelsall models 4myc, resolution 3.06Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4myc is a 3 chain structure with sequence from Saccharomyces cerevisiae S288C. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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