Publication Date:
2014-03-08
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Srinivasan, Vasundara -- Pierik, Antonio J -- Lill, Roland -- New York, N.Y. -- Science. 2014 Mar 7;343(6175):1137-40. doi: 10.1126/science.1246729.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut fur Zytobiologie, Philipps-Universitat Marburg, Robert-Koch-Strasse 6, 35032 Marburg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/24604199" target="_blank"〉PubMed〈/a〉
Keywords:
ATP-Binding Cassette Transporters/*chemistry
;
Adenosine Triphosphate/chemistry
;
Binding Sites
;
Crystallography, X-Ray
;
Glutathione/*chemistry
;
Mitochondria/*metabolism
;
Protein Multimerization
;
Protein Stability
;
Protein Structure, Secondary
;
Saccharomyces cerevisiae Proteins/*chemistry
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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