000148379 001__ 148379
000148379 005__ 20250730151142.0
000148379 0247_ $$2pmid$$apmid:23344952
000148379 0247_ $$2pmc$$apmc:PMC3605634
000148379 0247_ $$2doi$$a10.1074/jbc.M112.442285
000148379 0247_ $$2ISSN$$a1083-351X
000148379 0247_ $$2ISSN$$a0021-9258
000148379 0247_ $$2WOS$$aWOS:000316564500016
000148379 0247_ $$2altmetric$$aaltmetric:1194079
000148379 0247_ $$2openalex$$aopenalex:W2158989840
000148379 037__ $$aPHPPUBDB-26381
000148379 041__ $$aeng
000148379 082__ $$a570
000148379 1001_ $$aSoderberg, C. A. G.
000148379 1101_ $$aDESY$$bEuropean Molecular Biology Laboratory
000148379 245__ $$aThe Molecular Basis of Iron-induced Oligomerization of Frataxin and the Role of the Ferroxidation Reaction in Oligomerization
000148379 260__ $$aBethesda, Md.$$bSoc.$$c2013
000148379 300__ $$a8156
000148379 3367_ $$00$$2EndNote$$aJournal Article
000148379 3367_ $$2BibTeX$$aARTICLE
000148379 3367_ $$2DRIVER$$aarticle
000148379 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article$$mjournal
000148379 440_0 $$0PERI:(DE-600)1474604-9$$aJ. Biol. Chem.$$v288$$x0021-9258$$y12
000148379 500__ $$3POF3_Assignment on 2016-02-09
000148379 500__ $$3Converted on 2013-05-30 10:09
000148379 500__ $$3Converted on 2013-06-21 19:21
000148379 520__ $$aThe role of the mitochondrial protein frataxin in iron storage and detoxification, iron delivery to iron-sulfur cluster biosynthesis, heme biosynthesis, and aconitase repair has been extensively studied during the last decade. However, still no general consensus exists on the details of the mechanism of frataxin function and oligomerization. Here, using small-angle x-ray scattering and x-ray crystallography, we describe the solution structure of the oligomers formed during the iron-dependent assembly of yeast (Yfh1) and Escherichia coli (CyaY) frataxin. At an iron-to-protein ratio of 2, the initially monomeric Yfh1 is converted to a trimeric form in solution. The trimer in turn serves as the assembly unit for higher order oligomers induced at higher iron-to-protein ratios. The x-ray crystallographic structure obtained from iron-soaked crystals demonstrates that iron binds at the trimer-trimer interaction sites, presumably contributing to oligomer stabilization. For the ferroxidation-deficient D79A/D82A variant of Yfh1, iron-dependent oligomerization may still take place, although >50% of the protein is found in the monomeric state at the highest iron-to-protein ratio used. This demonstrates that the ferroxidation reaction controls frataxin assembly and presumably the iron chaperone function of frataxin and its interactions with target proteins. For E. coli CyaY, the assembly unit of higher order oligomers is a tetramer, which could be an effect of the much shorter N-terminal region of this protein. The results show that understanding of the mechanistic features of frataxin function requires detailed knowledge of the interplay between the ferroxidation reaction, iron-induced oligomerization, and the structure of oligomers formed during assembly.
000148379 536__ $$0G:(DE-H253)POF2-DORIS-PETRA-20130405$$aFacility (machine) DORIS/PETRA (POF2-DORIS-PETRA-20130405)$$cPOF2-DORIS-PETRA-20130405$$fPOF II$$x0
000148379 588__ $$aDataset connected to Pubmed
000148379 650_2 $$2MeSH$$aAmino Acid Sequence
000148379 650_2 $$2MeSH$$aAmino Acid Substitution
000148379 650_2 $$2MeSH$$aBinding Sites
000148379 650_2 $$2MeSH$$aConserved Sequence
000148379 650_2 $$2MeSH$$aCrystallography, X-Ray
000148379 650_2 $$2MeSH$$aEscherichia coli Proteins: chemistry
000148379 650_2 $$2MeSH$$aIron: chemistry
000148379 650_2 $$2MeSH$$aIron-Binding Proteins: chemistry
000148379 650_2 $$2MeSH$$aIron-Binding Proteins: genetics
000148379 650_2 $$2MeSH$$aModels, Molecular
000148379 650_2 $$2MeSH$$aMolecular Sequence Data
000148379 650_2 $$2MeSH$$aMutagenesis, Site-Directed
000148379 650_2 $$2MeSH$$aOxidation-Reduction
000148379 650_2 $$2MeSH$$aProtein Binding
000148379 650_2 $$2MeSH$$aProtein Interaction Domains and Motifs
000148379 650_2 $$2MeSH$$aProtein Multimerization
000148379 650_2 $$2MeSH$$aProtein Structure, Quaternary
000148379 650_2 $$2MeSH$$aProtein Structure, Secondary
000148379 650_2 $$2MeSH$$aScattering, Small Angle
000148379 650_2 $$2MeSH$$aThermodynamics
000148379 650_7 $$00$$2NLM Chemicals$$aCyaY protein, E coli
000148379 650_7 $$00$$2NLM Chemicals$$aEscherichia coli Proteins
000148379 650_7 $$00$$2NLM Chemicals$$aIron-Binding Proteins
000148379 650_7 $$00$$2NLM Chemicals$$afrataxin
000148379 650_7 $$07439-89-6$$2NLM Chemicals$$aIron
000148379 693__ $$0EXP:(DE-H253)DORISIII(machine)-20150101$$1EXP:(DE-H253)DORISIII-20150101$$5EXP:(DE-H253)DORISIII(machine)-20150101$$aDORIS III$$eFacility (machine) DORIS III$$x0
000148379 7001_ $$aRajan, S.
000148379 7001_ $$aShkumatov, A. V.
000148379 7001_ $$aGakh, O.
000148379 7001_ $$aSchaefer, S.
000148379 7001_ $$aAhlgren, E.-C.
000148379 7001_ $$aSvergun, D. I.
000148379 7001_ $$aIsaya, G.
000148379 7001_ $$aAl-karadaghi, S.
000148379 773__ $$0PERI:(DE-600)1474604-9$$a10.1074/jbc.M112.442285$$gVol. 288, p. 8156$$p8156$$q288<8156$$tThe @journal of biological chemistry$$v288$$x0021-9258$$y2013
000148379 8567_ $$2Pubmed Central$$uhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC3605634
000148379 909CO $$ooai:bib-pubdb1.desy.de:148379$$pVDB
000148379 9101_ $$0I:(DE-588b)2008985-5$$aDeutsches Elektronen-Synchrotron$$kDESY
000148379 9141_ $$y2013
000148379 915__ $$0StatID:(DE-HGF)0010$$aJCR/ISI refereed
000148379 915__ $$0StatID:(DE-HGF)0300$$2StatID$$aMedline
000148379 915__ $$0StatID:(DE-HGF)1$$2StatID$$aNo Author Disambiguation
000148379 9132_ $$0G:(DE-HGF)POF3-621$$1G:(DE-HGF)POF3-620$$2G:(DE-HGF)POF3-600$$9G:(DE-HGF)POF3-6215$$aDE-HGF$$bForschungsbereich Materie$$lVon Materie zu Materialien und Leben$$vIn-house research on the structure, dynamics and function of matter$$x0
000148379 9131_ $$0G:(DE-HGF)POF2-54G13$$1G:(DE-HGF)POF2-540$$2G:(DE-HGF)POF2-500$$9G:(DE-H253)POF2-DORIS-PETRA-20130405$$aDE-H253$$bStruktur der Materie$$lForschung mit Photonen, Neutronen und Ionen (PNI)$$vDORIS III$$x0
000148379 920_1 $$iExperiments with synchrotron radiation$$kHASYLAB
000148379 9201_ $$0I:(DE-H253)EMBL_-2012_-20130307$$kEMBL$$lEuropean Molecular Biology Laboratory$$x0
000148379 920__ $$k100
000148379 980__ $$aPHPPUBDB
000148379 980__ $$aVDB
000148379 980__ $$aUNRESTRICTED
000148379 980__ $$ajournal
000148379 980__ $$aI:(DE-H253)EMBL_-2012_-20130307
000148379 980__ $$aConvertedRecord