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Towards a structural understanding of Friedreich’s ataxia: the solution structure of frataxin
Open accessAbstract
Background Lesions in the gene for frataxin, a nuclear-encoded mitochondrial protein, cause the recessively inherited condition Friedreich's ataxia. It is thought that the condition arises from disregulation of mitochondrial iron homeostasis, with concomitant oxidative damage leading to neuronal death. Very little is, as yet, known about the biochemical function of frataxin. Results Here, we show that the mature form of recombinant frataxin behaves in solution as a monodisperse species that is composed of a 15-residue-long unstructured N terminus and an evolutionarily conserved C-terminal region that is able to fold independently. The structure of the C-terminal domain consists of a stable seven-stranded antiparallel beta sheet packing against a pair of parallel helices. The structure is compact with neither grooves nor cavities, features that are typical of iron-binding modules. Exposed evolutionarily conserved residues cover a broad area and all cluster on the beta-sheet face of the structure, suggesting that this is a functionally important surface. The effect of two clinically occurring mutations on the fold was checked experimentally. When the mature protein was titrated with iron, no tendency to iron-binding or to aggregation was observed. Conclusions Knowledge of the frataxin structure provides important guidelines as to the nature of the frataxin binding partner. The absence of all the features expected for an iron-binding activity, the large conserved area on its surface and lack of evidence for iron-binding activity strongly support an indirect involvement of frataxin in iron metabolism. The effects of point mutations associated with Friedreich's ataxia can be rationalised by knowledge of the structure and suggest possible models for the occurrence of the disease in compound heterozygous patients.
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“It negatively regulates iron efflux by binding Fpn and triggering its internalization and subsequent degradation (215).”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [215]
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“Fpn is posttranslationally regulated by a peptide hormone, hepcidin (215).”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [215]
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“Over-expression of Fpn accelerates export of cytosolic iron (215)”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [215]
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Citations
Cites
Thompson, J. (1997) · Nucleic Acids Research · doi:10.1093/nar/25.24.4876 · Cited by 38,685
AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
Laskowski, R., Rullmann, J. A., MacArthur, M., Kaptein, R., & Thornton, J. (1996) · Journal of Biomolecular NMR · doi:10.1007/bf00228148 · Cited by 5,502
WHAT IF: A molecular modeling and drug design program
Vriend, G. (1990) · Journal of Molecular Graphics · doi:10.1016/0263-7855(90)80070-v · Cited by 3,476
Friedreich's Ataxia: Autosomal Recessive Disease Caused by an Intronic GAA Triplet Repeat Expansion
Campuzano, V., Montermini, L., Moltò, M. D., Pianese, L., Cossée, M., Cavalcanti, F., Monros, E., Rodius, F., Duclos, F., Monticelli, A., et al. (1996) · Science · doi:10.1126/science.271.5254.1423 · Cited by 2,786
Torsion angle dynamics for NMR structure calculation with the new program Dyana
Güntert, P., Mumenthaler, C., & Kurt Wüthrich, A. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.1284 · Cited by 2,781
The ferritins: molecular properties, iron storage function and cellular regulation
Harrison, P. M., & Arosio, P. (1996) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(96)00022-9 · Cited by 2,667
Recognition of errors in three‐dimensional structures of proteins
Sippl, M. J. (1993) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340170404 · Cited by 2,156
Clinical and Genetic Abnormalities in Patients with Friedreich's Ataxia
Dürr, A., Cossee, M., Agid, Y., Campuzano, V., Mignard, C., Penet, C., Mandel, J.-L., Brice, A., & Koenig, M. (1996) · New England Journal of Medicine · doi:10.1056/nejm199610173351601 · Cited by 1,071
Aconitase and mitochondrial iron–sulphur protein deficiency in Friedreich ataxia
Rötig, A., de Lonlay, P., Chretien, D., Foury, F., Koenig, M., Sidi, D., Munnich, A., & Rustin, P. (1997) · Nature Genetics · doi:10.1038/ng1097-215 · Cited by 991
Regulation of Mitochondrial Iron Accumulation by Yfh1p, a Putative Homolog of Frataxin
Babcock, M., de Silva, D., Oaks, R., Davis-Kaplan, S., Jiralerspong, S., Montermini, L., Pandolfo, M., & Kaplan, J. (1997) · Science · doi:10.1126/science.276.5319.1709 · Cited by 921
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Télot, L., Rousseau, E., Lesuisse, E., Garcia, C., Morlet, B., Léger, T., Camadro, J., & Serre, V. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2018.01.010 · Cited by 25
The N‐terminus of mature human frataxin is intrinsically unfolded
Prischi, F., Giannini, C., Adinolfi, S., & Pastore, A. (2009) · FEBS Journal · doi:10.1111/j.1742-4658.2009.07381.x · Cited by 24
Self-citationHuman Frataxin Folds Via an Intermediate State. Role of the C-Terminal Region
Faraj, S. E., González‐Lebrero, R. M., Román, E. A., & Santos, J. (2016) · Scientific Reports · doi:10.1038/srep20782 · Cited by 24
Bellanda, M., Maso, L., Doni, D., Bortolus, M., Rosa, E. D., Lunardi, F., Alfonsi, A., Noguera, M. E., Herrera, M. G., Santos, J., et al. (2019) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2019.07.007 · Cited by 23
Expression and one-step purification of recombinant Arabidopsis thaliana frataxin homolog (AtFH)
Maliandi, M. V., Busi, M. V., Clemente, M., Zabaleta, E. J., Araya, A., & Gomez‐Casati, D. F. (2006) · Protein Expression and Purification · doi:10.1016/j.pep.2006.06.007 · Cited by 23
Iron Pathophysiology in Friedreich’s Ataxia
Li, K. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-13-9589-5_7 · Cited by 22
Correlation of 2J couplings with protein secondary structure
Schmidt, J. M., Hua, Y., & Löhr, F. (2009) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.22672 · Cited by 21
Popovic, M., Sanfelice, D., Pastore, C., Prischi, F., Temussi, P. A., & Pastore, A. (2015) · Protein Science · doi:10.1002/pro.2679 · Cited by 20
Self-citationThe kinetics of folding of frataxin
Bonetti, D., Toto, A., Giri, R., Morrone, A., Sanfelice, D., Pastore, A., Temussi, P. A., Gianni, S., & Brunori, M. (2014) · Physical Chemistry Chemical Physics · doi:10.1039/c3cp54055c · Cited by 20
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Masino, L., & Pastore, A. (2001) · Brain Research Bulletin · doi:10.1016/s0361-9230(01)00582-2 · Cited by 19
Self-citationDoni, D., Rigoni, G., Palumbo, E., Baschiera, E., Peruzzo, R., Rosa, E. D., Caicci, F., Passerini, L., Bettio, D., Russo, A., et al. (2021) · The FASEB Journal · doi:10.1096/fj.202000524rr · Cited by 19
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Faggianelli, N., Puglisi, R., Veneziano, L., Romano, S., Frontali, M., Vannocci, T., Fortuni, S., Testi, R., & Pastore, A. (2015) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2015.00066 · Cited by 17
“About 20 different point mutations are currently known (Musco et al., 2000; Correia et al., 2006), some of which accounting for atypical clinical presentations.”
BackgroundMethodInfluentialSelf-citationProtein Mutations and Stability, a Link with Disease: The Case Study of Frataxin
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“The three orthologues have a C-terminal tail with different lengths, without elements of a secondary structure [7,94] and with a higher mobility compared to the rest of the molecule, as confirmed by the smaller than average T1/T2 and small or negative NOE values [95], in agreement with larger rmsd of the solution bund…”
BackgroundInfluentialRecipes for Inducing Cold Denaturation in an Otherwise Stable Protein
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Self-citationRomán, E. A., Faraj, S. E., Cousido-Siah, A., Mitschler, A., PODJARNY, A. D., & Santos, J. (2013) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2013.02.015 · Cited by 15
“The average native structure of FXN has already been solved by NMR and crystallography [19,23,24] showing an αβ fold with a five-stranded antiparallel β sheet that forms a flat platform and two parallel α-helices that are tightly packed against it, forming an αβ sandwich.”
BackgroundDoni, D., Passerini, L., Audran, G., Marque, S. R. A., Schulz, M., Santos, J., Costantini, P., Bortolus, M., & Carbonera, D. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21249619 · Cited by 14
Correia, A. R., Ow, S. Y., Wright, P. C., & Gomes, C. M. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.10.095 · Cited by 14
“Frataxin core (91–210), from here on simply FXN, keeps the protein fold, stability and functional properties of the mature variant [16] and was used in this study.”
Cai, K., & Markley, J. L. (2018) · Molecules · doi:10.3390/molecules23092213 · Cited by 15
The role of the N-terminal tail for the oligomerization, folding and stability of human frataxin
Faraj, S., Venturutti, L., Román, E. A., Marino-Buslje, C., Mignone, A., Tosatto, S., Delfino, J., & Santos, J. (2013) · FEBS Open Bio · doi:10.1016/j.fob.2013.07.004 · Cited by 12
“The 3D structure of hFXN has been determined by X–ray crystallography [11] and by NMR [12] and its backbone dynamics has been thoroughly analyzed by NMR [13].”
MethodInfluentialThe role of frataxin in fission yeast iron metabolism: Implications for Friedreich's ataxia
Wang, Y., Wang, Y., Marcus, S., & Busenlehner, L. S. (2014) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2014.06.017 · Cited by 12
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Roumestand, C., Dudás, E. F., Puglisi, R., Caliò, A., Barthe, P., Temussi, P. A., & Pastore, A. (2025) · JACS Au · doi:10.1021/jacsau.5c00185 · Cited by 11
Self-citationStructural characterization of metal binding to a cold-adapted frataxin
Noguera, M. E., Román, E. A., Rigal, J. B., Cousido-Siah, A., Mitschler, A., PODJARNY, A. D., & Santos, J. (2015) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-015-1251-9 · Cited by 11
Insights on the conformational dynamics of human frataxin through modifications of loop-1
Noguera, M. E., Arán, M., Smal, C., Vazquez, D. S., Herrera, M. G., Román, E. A., Alaimo, N., Gallo, M. L., & Santos, J. (2017) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2017.10.022 · Cited by 10
Frataxins Emerge as New Players of the Intracellular Antioxidant Machinery
Uceda, A. B., Donoso, J., Frau, J., Vilanova, B., & Adrover, M. (2021) · Antioxidants · doi:10.3390/antiox10020315 · Cited by 9
“The C-terminal domain of human frataxin (91–210; Hfra) was expressed in E. coli BL21(DE3) as fusion protein with a His-tagged glutathione S -transferase (GST) and a cleave site for PreScission protease, as described previously [8].”
InfluentialNMR assignments of a stable processing intermediate of human frataxin
Kondapalli, K. C., Bencze, K. Z., Dizin, E., Cowan, J. A., & Stemmler, T. L. (2010) · Biomolecular NMR Assignments · doi:10.1007/s12104-010-9209-x · Cited by 8
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Rasheed, M., Jamshidiha, M., Puglisi, R., Yan, R., Cota, E., & Pastore, A. (2019) · FEBS Journal · doi:10.1111/febs.14750 · Cited by 6
Self-citationWatson, H. M., Gentry, L. E., Asuru, A. P., Wang, Y., Marcus, S., & Busenlehner, L. S. (2012) · Biochemistry · doi:10.1021/bi300779f · Cited by 5
Selection of synthetic proteins to modulate the human frataxin function
Pignataro, M. F., Herrera, M. G., Fernández, N., Arán, M., Gentili, H., Battaglini, F., & Santos, J. (2022) · Biotechnology and Bioengineering · doi:10.1002/bit.28263 · Cited by 5
“The structure of the human frataxin has been obtained by crystallography [13] and NMR [14, 15].”
BackgroundResultInfluentialDoni, D., Meggiolaro, M., Santos, J., Audran, G., Marque, S. R. A., Costantini, P., Bortolus, M., & Carbonera, D. (2021) · Biomedicines · doi:10.3390/biomedicines9121763 · Cited by 5
“Residues 81–92 of the N-terminal portion are intrinsically unfolded [13] and are often partially truncated for in vitro studies [14] to obtain FXN 90–210.”
BackgroundModelling Protein Plasticity: The Example of Frataxin and Its Variants
Botticelli, S., Penna, G. L., Nobili, G., Rossi, G. C., Stellato, F., & Morante, S. (2022) · Molecules · doi:10.3390/molecules27061955 · Cited by 5
“The backbone root-mean square deviation (RMSD) (see Section 5) is a rough indication of the change in backbone structure RMSD values calculated between the 15 different models obtained for FXN in the 90-210 truncated form by solution NMR (PDB 1LY7 [24]) are in the range 1.”
MethodCorreia, A. R., Naik, S., Fisher, M. T., & Gomes, C. M. (2014) · Biomolecules · doi:10.3390/biom4040956 · Cited by 5
“All constructs were expressed in Escherichia coli competent cells (BL21 (DE3)) and the frataxin protein was purified as previously described [10,50,51].”
MethodThermodynamic Stabilization of Human FrataxinPreprint
Núñez‐Franco, R., Torres-Mozas, Á., Navo, C. D., Schedlbauer, A., Azkargorta, M., Iloro, I., Elortza, F., Ortega, G., Millet, Ó., Peccati, F., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.09.08.556816 · Cited by 5
Life and death of Yfh1: how cool is cold denaturation
Temussi, P. A., Martin, S. R., & Pastore, A. (2025) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583524000180 · Cited by 4
“In 2010, Correia et al. reported the characterisation of eight Yfh1 variants affecting residues in the α 1/ β 1 acidic ridge identified in Musco et al. (2000) and the conserved β -sheet surface (Correia et al., 2010).”
InfluentialSelf-citationProtoporphyrin IX Binds to Iron(II)-Loaded and to Zinc-Loaded Human Frataxin
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“This binding scenario is consistent with the large number of aspartic and glutamic residues in FXN, distributed across all the secondary structural elements [1] and it also provides a structural rationale for the elevated number of ferrous ions simultaneously coordinated by the protein [15].”
BackgroundMethodInfluentialProtein structure determination using a Riemannian approach
Wei, X., Li, Z., Li, S., Peng, X., & Zhao, Q. B. (2019) · FEBS Letters · doi:10.1002/1873-3468.13688 · Cited by 4
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Self-citationPandolfo, M. (2007) · Springer eBooks · doi:10.1007/3-540-33336-3_4 · Cited by 3
Terenzi, A., Pagani, M. A., Gomez‐Casati, D. F., & Busi, M. V. (2022) · Plants · doi:10.3390/plants11151931 · Cited by 3
Conceição, L. M. A. D., Cabral, L. M., Pereira, G. R. C., & Mesquita, J. F. D. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25115796 · Cited by 5
“Given the key role of the N-terminal domain in protein maturation through interactions with MPP, these mutations may hinder FXN’s recognition, thus impacting the cleavage steps involved in its maturation, aligning with the findings of the previous literature [58,59,72,76–78].”
ResultDoni, D., Cavallari, E., Noguera, M. E., Gentili, H., Cavion, F., Parisi, G. D., Fornasari, M. S., Sartori, G., Santos, J., Bellanda, M., et al. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25031912 · Cited by 2
“Nqo15 adopts the FXN fold, and a comparison of FXN homologues from different organisms reveals a high degree of structural similarity, all sharing an α - β sandwich motif with two α -helices packing six-to seven-stranded β -sheets [25,26,29,30].”
BackgroundMethodAnimal Models of Friedreich Ataxia
Pandolfo, M. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-405195-9.00065-2 · Cited by 2
Kırboğa, K. K., & Küçüksille, E. U. (2026) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.6c00960 · Cited by 1
Chemical shift assignment of a thermophile frataxin
Rasheed, M., Yan, R., Kelly, G. P., & Pastore, A. (2017) · Biomolecular NMR Assignments · doi:10.1007/s12104-017-9790-3 · Cited by 1
“The protein was further purified by a second Ni-affinity step followed by FPLC size-exclusion chromatography (Superdex 75, GE Healthcare) as previously described (Musco et al. 2000).”
BackgroundMethodSelf-citationPandolfo, M. (2003) · Elsevier eBooks · doi:10.1016/b978-012566652-7/50020-4 · Cited by 1
Shafiei, A., Baldir, N., Na, J., Kim, J. H., & DeMi̇rci̇, H. (2025) · ChemBioChem · doi:10.1002/cbic.202500442 · Cited by 1
PROTEIN FOLDING AND DISEASE THE MITOCHONDRIAL PROTEIN FRATAXIN
Correia, A. R. (2010) · Portuguese National Funding Agency for Science, Research and Technology (RCAAP Project by FCT)
Using Comparative Genome Analysis to Find Interaction Partners for Frataxin
Huynen, M. A. (2002) · Developments in cardiovascular medicine · doi:10.1007/978-1-4615-1005-5_4
Characterization of poly (rc) binding protein (pcbp2) and frataxin
Ghimire-Rijal, S. (2011) · Human Biology
Friedreich's Ataxia and Diseases Associated with Expansion of Non‐Coding Triplets
Crichton, R. R., & Ward, R. J. (2005) · doi:10.1002/0470022574.ch6
Pandolfo, M. (2007) · Blue books of neurology · doi:10.1016/s1877-184x(09)70081-4
DEFINITION OF THE LANDSCAPE OF CHROMATIN STRUCTURE AT THE FRATAXIN GENE IN FRIEDREICH’S ATAXIA
Kim, E. (2011) · Digital Commons-TMC (Texas Medical Center)
Marmolino, D., & Pandolfo, M. (2011) · Dépôt institutionnel de l'Université libre de Bruxelles (Université Libre de Bruxelles)
Mutations causing Friedreich ataxia
Pandolfo, M. (2007) · Future Neurology · doi:10.2217/14796708.3.1.73
“Structurally, mature frataxin is a compact, globular protein containing an N-terminal α-helix, a middle β-sheet region composed of seven β strands, a second α-helix, and a C-terminus in an extended conformation [25].”
BackgroundPastore, A. (2013) · Royal Society of Chemistry eBooks · doi:10.1039/9781849735896-00098
Self-citationFriedreich's ataxia and other autosomal recessive ataxias
Puccio, H. M., & Koenig, M. (2005) · Cambridge University Press eBooks · doi:10.1017/cbo9780511544873.049
Animal Models of Friedreich Ataxia
Pandolfo, M. (2005) · Elsevier eBooks · doi:10.1016/b978-012088382-0/50057-8
Friedreich's Ataxia and Diseases Associated with Expansion of Non‐Coding Triplets
Crichton, R. R., & Ward, R. J. (2013) · doi:10.1002/9781118553480.ch09
Roumestand, C., Dudás, E. F., Puglisi, R., Caliò, A., Barthe, P., Temussi, P. A., & Pastore, A. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.07.15.603545
“The Yfh1 fold consists of two N-and C-terminal helices that pack on the same side against a 5-7 strand -sheet depending on the ortholog (Musco et al., 2000).”
BackgroundSelf-citationComputational analysis of evolutionary and structural aspects of Cryptochromes and Frataxins
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PathDiffusion: modeling protein folding pathway using evolution-guided diffusionPreprint
Zhao, K. B., Xiang, C., Cheng, B., Shen, Y., Wang, W., Chen, S., Su, B., Zhang, G., Peng, Z., & Yang, J. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.01.16.699856
Etude du rôle de la frataxine bactérienne CyaY chez Escherichia coli
Roche, B. (2015) · theses.fr (ABES) · doi:10.70675/0cfc0f0ez98c2z41c3z974azcfccad1c77a9
Identification of therapeutic strategies on new Drosophila models of Friedreich's ataxia
Russi, M. (2020) · theses.fr (ABES) · doi:10.70675/3e527a1fz003bz4d84z9b06z614b9b0c0821
Contrôle de la résistance aux antibiotiques par des ARN régulateurs
Baussier, C. (2023) · theses.fr (ABES) · doi:10.70675/f49c0a6bz58a5z4e8fz8691z0e7220d5adab
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Self-citationOxidative Stress and Friedreich’s Ataxia
Bolotta, A. (2014) · AMS Dottorato Institutional Doctoral Theses Repository (University of Bologna) · doi:10.6092/unibo/amsdottorato/6282
Metadata
- Authors
- Musco, G., Stier, G., Kolmerer, B., Adinolfi, S., Martin, S., Frenkiel, T., Gibson, T., & Pastore, A.
- Affiliations
- European Molecular Biology Laboratory (DE)
- Corresponding author
- Pastore, Annalisa
- Venue
- Structure
- Publisher
- Elsevier BV
- Published
- 2000-07
- Volume
- 8
- Issue
- 7
- Pages
- 695-707
- ISSN
- 0969-2126 (ISSN-L)
- OpenAlex
- W2043666185
- Cited by
- 166
- References
- 53
- Citations by year
- 2026: 3 · 2025: 3 · 2024: 3 · 2023: 5 · 2022: 9 · 2021: 4 · 2020: 4 · 2019: 4 · 2018: 6 · 2017: 3 · 2016: 3 · 2015: 6 · 2014: 11 · 2013: 9 · 2012: 3
- FWCI
- 3.62
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Structure (publishedVersion)
- PubMed (publishedVersion)
- Institutional Research Information System University of Turin (University of Turin) (submittedVersion, other-oa)
- Max Planck Institute for Plasma Physics (submittedVersion)
- Max Planck Digital Library (submittedVersion)
- MPG.PuRe (Max Planck Society) (submittedVersion)
- Scuola Normale Superiore di Pisa (submittedVersion)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Genetic Neurodegenerative Diseases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Keywords
- Friedreich's ataxia, frataxin, protein solution structure, mitochondrial iron homeostasis, C-terminal domain, antiparallel beta-sheet, point mutations, compound heterozygosity, protein aggregation
- MeSH terms
- Frataxin, Amino Acid Sequence, Animals, Bacterial Proteins, Carrier Proteins, Circular Dichroism, Friedreich Ataxia, Fungal Proteins, Heterozygote, Humans, Iron, Ligands, Mitochondria, Models, Molecular, Molecular Sequence Data, Plant Proteins, Protein Conformation, Recombinant Fusion Proteins, Species Specificity, Structure-Activity Relationship, Helminth Proteins, Sequence Alignment, Point Mutation, Sequence Homology, Amino Acid, Protein Structure, Secondary, Phosphotransferases (Alcohol Group Acceptor), Oxidative Stress, Evolution, Molecular, Iron-Binding Proteins, Transferrin-Binding Proteins, Mice
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