%0 Journal Article
%A Soderberg, C. A. G.
%A Rajan, S.
%A Shkumatov, A. V.
%A Gakh, O.
%A Schaefer, S.
%A Ahlgren, E.-C.
%A Svergun, D. I.
%A Isaya, G.
%A Al-karadaghi, S.
%A DESY
%T The Molecular Basis of Iron-induced Oligomerization of Frataxin and the Role of the Ferroxidation Reaction in Oligomerization
%J The journal of biological chemistry
%V 288
%@ 0021-9258
%C Bethesda, Md.
%I Soc.
%M PHPPUBDB-26381
%P 8156
%D 2013
%X 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
%K Amino Acid Sequence
%K Amino Acid Substitution
%K Binding Sites
%K Conserved Sequence
%K Crystallography, X-Ray
%K Escherichia coli Proteins: chemistry
%K Iron: chemistry
%K Iron-Binding Proteins: chemistry
%K Iron-Binding Proteins: genetics
%K Models, Molecular
%K Molecular Sequence Data
%K Mutagenesis, Site-Directed
%K Oxidation-Reduction
%K Protein Binding
%K Protein Interaction Domains and Motifs
%K Protein Multimerization
%K Protein Structure, Quaternary
%K Protein Structure, Secondary
%K Scattering, Small Angle
%K Thermodynamics
%K CyaY protein, E coli (NLM Chemicals)
%K Escherichia coli Proteins (NLM Chemicals)
%K Iron-Binding Proteins (NLM Chemicals)
%K frataxin (NLM Chemicals)
%K Iron (NLM Chemicals)
%F PUB:(DE-HGF)16
%9 Journal Article
%$ pmid:23344952
%2 pmc:PMC3605634
%U <Go to ISI:>//WOS:000316564500016
%R 10.1074/jbc.M112.442285
%U https://bib-pubdb1.desy.de/record/148379