TY  - JOUR
AU  - Soderberg, C. A. G.
AU  - Rajan, S.
AU  - Shkumatov, A. V.
AU  - Gakh, O.
AU  - Schaefer, S.
AU  - Ahlgren, E.-C.
AU  - Svergun, D. I.
AU  - Isaya, G.
AU  - Al-karadaghi, S.
AU  - DESY
TI  - The Molecular Basis of Iron-induced Oligomerization of Frataxin and the Role of the Ferroxidation Reaction in Oligomerization
JO  - The journal of biological chemistry
VL  - 288
SN  - 0021-9258
CY  - Bethesda, Md.
PB  - Soc.
M1  - PHPPUBDB-26381
SP  - 8156
PY  - 2013
AB  - 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
KW  - Amino Acid Sequence
KW  - Amino Acid Substitution
KW  - Binding Sites
KW  - Conserved Sequence
KW  - Crystallography, X-Ray
KW  - Escherichia coli Proteins: chemistry
KW  - Iron: chemistry
KW  - Iron-Binding Proteins: chemistry
KW  - Iron-Binding Proteins: genetics
KW  - Models, Molecular
KW  - Molecular Sequence Data
KW  - Mutagenesis, Site-Directed
KW  - Oxidation-Reduction
KW  - Protein Binding
KW  - Protein Interaction Domains and Motifs
KW  - Protein Multimerization
KW  - Protein Structure, Quaternary
KW  - Protein Structure, Secondary
KW  - Scattering, Small Angle
KW  - Thermodynamics
KW  - CyaY protein, E coli (NLM Chemicals)
KW  - Escherichia coli Proteins (NLM Chemicals)
KW  - Iron-Binding Proteins (NLM Chemicals)
KW  - frataxin (NLM Chemicals)
KW  - Iron (NLM Chemicals)
LB  - PUB:(DE-HGF)16
C6  - pmid:23344952
C2  - pmc:PMC3605634
UR  - <Go to ISI:>//WOS:000316564500016
DO  - DOI:10.1074/jbc.M112.442285
UR  - https://bib-pubdb1.desy.de/record/148379
ER  -