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PDBsum entry 4myh
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Transport protein
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PDB id
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4myh
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PDB id:
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| Name: |
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Transport protein
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Title:
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Structure of the glutathione bound mitochondrial abc transporter, atm1
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Structure:
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Iron-sulfur clusters transporter atm1, mitochondrial. Chain: a, c, b. Fragment: unp residues 98-690. Engineered: yes
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Source:
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Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 559292. Strain: atcc 204508 / s288c. Gene: atm1, mdy, ymr301c, ym9952.03c. Expressed in: escherichia coli. Expression_system_taxid: 562
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Resolution:
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3.38Å
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R-factor:
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0.250
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R-free:
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0.290
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Authors:
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V.Srinivasan
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Key ref:
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V.Srinivasan
et al.
(2014).
Crystal structures of nucleotide-free and glutathione-bound mitochondrial ABC transporter Atm1.
Science,
343,
1137-1140.
PubMed id:
DOI:
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Date:
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27-Sep-13
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Release date:
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26-Mar-14
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PROCHECK
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Headers
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References
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P40416
(ATM1_YEAST) -
Iron-sulfur clusters transporter ATM1, mitochondrial from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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Seq:
Struc:
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690 a.a.
598 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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DOI no:
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Science
343:1137-1140
(2014)
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PubMed id:
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Crystal structures of nucleotide-free and glutathione-bound mitochondrial ABC transporter Atm1.
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V.Srinivasan,
A.J.Pierik,
R.Lill.
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ABSTRACT
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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 α-helices of the Atm1
dimer. The resulting protein stabilization may be a common structural feature of
all ABC exporters.
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Links
