4MYH

Structure of the Glutathione bound mitochondrial ABC transporter, Atm1

Summary for 4MYH

• Entry DOI: 10.2210/pdb4myh/pdb
• Related: 4MYC
• Descriptor: Iron-sulfur clusters transporter ATM1, mitochondrial, GLUTATHIONE (2 entities in total)
• Functional Keywords: abc transporter, membrane transport, mitochondrial inner membrane, glutathione, transport protein
• Biological source: Saccharomyces cerevisiae (Baker's yeast)
• Cellular location: Mitochondrion inner membrane ; Multi- pass membrane protein : P40416
• Total number of polymer chains: 3
• Total formula weight: 201944.96

Authors

Srinivasan, V. (deposition date: 2013-09-27, release date: 2014-03-26, Last modification date: 2024-02-28)

Primary citation

Srinivasan, V.,Pierik, A.J.,Lill, R.
Crystal structures of nucleotide-free and glutathione-bound mitochondrial ABC transporter Atm1.
Science, 343:1137-1140, 2014

PubMed Abstract: 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 α-helices of the Atm1 dimer. The resulting protein stabilization may be a common structural feature of all ABC exporters.

PubMed: 24604199
DOI: 10.1126/science.1246729

Experimental method

X-RAY DIFFRACTION (3.38 Å)