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@ARTICLE{Soderberg:148379,
      author       = {Soderberg, C. A. G. and Rajan, S. and Shkumatov, A. V. and
                      Gakh, O. and Schaefer, S. and Ahlgren, E.-C. and Svergun, D.
                      I. and Isaya, G. and Al-karadaghi, S. and DESY},
      title        = {{T}he {M}olecular {B}asis of {I}ron-induced
                      {O}ligomerization of {F}rataxin and the {R}ole of the
                      {F}erroxidation {R}eaction in {O}ligomerization},
      journal      = {The journal of biological chemistry},
      volume       = {288},
      issn         = {0021-9258},
      address      = {Bethesda, Md.},
      publisher    = {Soc.},
      reportid     = {PHPPUBDB-26381},
      pages        = {8156},
      year         = {2013},
      abstract     = {The role of the mitochondrial protein frataxin in iron
                      storage and detoxification, iron delivery to iron-sulfur
                      cluster biosynthesis, heme biosynthesis, and aconitase
                      repair has been extensively studied during the last decade.
                      However, still no general consensus exists on the details of
                      the mechanism of frataxin function and oligomerization.
                      Here, using small-angle x-ray scattering and x-ray
                      crystallography, we describe the solution structure of the
                      oligomers formed during the iron-dependent assembly of yeast
                      (Yfh1) and Escherichia coli (CyaY) frataxin. At an
                      iron-to-protein ratio of 2, the initially monomeric Yfh1 is
                      converted to a trimeric form in solution. The trimer in turn
                      serves as the assembly unit for higher order oligomers
                      induced at higher iron-to-protein ratios. The x-ray
                      crystallographic structure obtained from iron-soaked
                      crystals demonstrates that iron binds at the trimer-trimer
                      interaction sites, presumably contributing to oligomer
                      stabilization. For the ferroxidation-deficient D79A/D82A
                      variant of Yfh1, iron-dependent oligomerization may still
                      take place, although $>50\%$ of the protein is found in the
                      monomeric state at the highest iron-to-protein ratio used.
                      This demonstrates that the ferroxidation reaction controls
                      frataxin assembly and presumably the iron chaperone function
                      of frataxin and its interactions with target proteins. For
                      E. coli CyaY, the assembly unit of higher order oligomers is
                      a tetramer, which could be an effect of the much shorter
                      N-terminal region of this protein. The results show that
                      understanding of the mechanistic features of frataxin
                      function requires detailed knowledge of the interplay
                      between the ferroxidation reaction, iron-induced
                      oligomerization, and the structure of oligomers formed
                      during assembly.},
      keywords     = {Amino Acid Sequence / Amino Acid Substitution / Binding
                      Sites / Conserved Sequence / Crystallography, X-Ray /
                      Escherichia coli Proteins: chemistry / Iron: chemistry /
                      Iron-Binding Proteins: chemistry / Iron-Binding Proteins:
                      genetics / Models, Molecular / Molecular Sequence Data /
                      Mutagenesis, Site-Directed / Oxidation-Reduction / Protein
                      Binding / Protein Interaction Domains and Motifs / Protein
                      Multimerization / Protein Structure, Quaternary / Protein
                      Structure, Secondary / Scattering, Small Angle /
                      Thermodynamics / CyaY protein, E coli (NLM Chemicals) /
                      Escherichia coli Proteins (NLM Chemicals) / Iron-Binding
                      Proteins (NLM Chemicals) / frataxin (NLM Chemicals) / Iron
                      (NLM Chemicals)},
      cin          = {EMBL},
      ddc          = {570},
      cid          = {$I:(DE-H253)EMBL_-2012_-20130307$},
      pnm          = {Facility (machine) DORIS/PETRA (POF2-DORIS-PETRA-20130405)},
      pid          = {G:(DE-H253)POF2-DORIS-PETRA-20130405},
      experiment   = {EXP:(DE-H253)DORISIII(machine)-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:23344952},
      pmc          = {pmc:PMC3605634},
      UT           = {WOS:000316564500016},
      doi          = {10.1074/jbc.M112.442285},
      url          = {https://bib-pubdb1.desy.de/record/148379},
}