메뉴 건너뛰기




Volumn 12, Issue 11, 2004, Pages 2037-2048

Solution structure of the bacterial frataxin ortholog, CyaY: Mapping the iron binding sites

Author keywords

[No Author keywords available]

Indexed keywords

FERRIC ION; FERROUS ION; FRATAXIN;

EID: 7944225865     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2004.08.012     Document Type: Article
Times cited : (120)

References (54)
  • 2
    • 0036667986 scopus 로고    scopus 로고
    • A structural approach to understanding the iron-binding properties of phylogenetically different frataxins
    • Adinolfi S., Trifuoggi M., Politou A.S., Martin S., Pastore A. A structural approach to understanding the iron-binding properties of phylogenetically different frataxins. Hum. Mol. Genet. 11:2002;1865-1877
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 1865-1877
    • Adinolfi, S.1    Trifuoggi, M.2    Politou, A.S.3    Martin, S.4    Pastore, A.5
  • 3
    • 2542542239 scopus 로고    scopus 로고
    • The factors governing the thermal stability of frataxin orthologues: How to increase a protein stability
    • Adinolfi S., Nair M., Politou A., Bayer E., Martin S., Temussi P., Pastore A. The factors governing the thermal stability of frataxin orthologues. how to increase a protein stability Biochemistry. 43:2004;6511-6518
    • (2004) Biochemistry , vol.43 , pp. 6511-6518
    • Adinolfi, S.1    Nair, M.2    Politou, A.3    Bayer, E.4    Martin, S.5    Temussi, P.6    Pastore, A.7
  • 4
    • 0034636795 scopus 로고    scopus 로고
    • IscU as a scaffold for iron-sulfur cluster biosynthesis: Sequential assembly of [2Fe-2S] and [4Fe-4S] clusters in IscU
    • Agar J.N., Krebs C., Frazzon J., Huynh B.H., Dean D.R., Johnson M.K. IscU as a scaffold for iron-sulfur cluster biosynthesis. sequential assembly of [2Fe-2S] and [4Fe-4S] clusters in IscU Biochemistry. 39:2000;7856-7862
    • (2000) Biochemistry , vol.39 , pp. 7856-7862
    • Agar, J.N.1    Krebs, C.2    Frazzon, J.3    Huynh, B.H.4    Dean, D.R.5    Johnson, M.K.6
  • 6
    • 0343459675 scopus 로고
    • The program XEASY for computer-supported NMR spectral analysis of biological macromolecules
    • Bartels C.H., Xia T.-H., Billeter M., Güntert P., Wüthrich K. The program XEASY for computer-supported NMR spectral analysis of biological macromolecules. J. Biomol. NMR. 5:1995;1-10
    • (1995) J. Biomol. NMR , vol.5 , pp. 1-10
    • Bartels, C.H.1    Xia, T.-H.2    Billeter, M.3    Güntert, P.4    Wüthrich, K.5
  • 8
    • 3342981572 scopus 로고    scopus 로고
    • Iron binding and oxidation properties of the bacterial frataxin Cyay of Escherichia coli
    • Bou-Abdallah F., Adinolfi S., Pastore A., Laue T.M., Chasteen D.N. Iron binding and oxidation properties of the bacterial frataxin Cyay of Escherichia coli. J. Mol. Biol. 341:2004;605-615
    • (2004) J. Mol. Biol. , vol.341 , pp. 605-615
    • Bou-Abdallah, F.1    Adinolfi, S.2    Pastore, A.3    Laue, T.M.4    Chasteen, D.N.5
  • 10
    • 3042763187 scopus 로고    scopus 로고
    • Frataxin actds as an iron chaperone protein to modulate mitochondrial aconitase activity
    • Bulteau A.L., O'Neill H.A., Kennedy M.C., Ikeda-Saito M., Isaya G., Szweda L.I. Frataxin actds as an iron chaperone protein to modulate mitochondrial aconitase activity. Science. 305:2004;242-245
    • (2004) Science , vol.305 , pp. 242-245
    • Bulteau, A.L.1    O'Neill, H.A.2    Kennedy, M.C.3    Ikeda-Saito, M.4    Isaya, G.5    Szweda, L.I.6
  • 11
    • 0022450133 scopus 로고
    • Amino-aromatic interactions in proteins
    • Burley S.K., Petsko G.A. Amino-aromatic interactions in proteins. FEBS Lett. 203:1986;139-143
    • (1986) FEBS Lett. , vol.203 , pp. 139-143
    • Burley, S.K.1    Petsko, G.A.2
  • 14
    • 0036472291 scopus 로고    scopus 로고
    • Assembly and iron-binding properties of human frataxin, the protein deficient in Friedreich ataxia
    • Cavadini P., O'Neill H.A., Benada O., Isaya G. Assembly and iron-binding properties of human frataxin, the protein deficient in Friedreich ataxia. Hum. Mol. Genet. 11:2002;217-227
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 217-227
    • Cavadini, P.1    O'Neill, H.A.2    Benada, O.3    Isaya, G.4
  • 15
    • 12944257432 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli CyaY protein reveals a previously unidentified fold for the evolutionarily conserved frataxin family
    • Cho S.J., Lee M.G., Yang J.K., Lee J.Y., Song H.K., Suh S.W. Crystal structure of Escherichia coli CyaY protein reveals a previously unidentified fold for the evolutionarily conserved frataxin family. Proc. Natl. Acad. Sci. USA. 97:2000;8932-8937
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 8932-8937
    • Cho, S.J.1    Lee, M.G.2    Yang, J.K.3    Lee, J.Y.4    Song, H.K.5    Suh, S.W.6
  • 16
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • Cornilescu G., Delaglio F., Bax A. Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J. Biomol. NMR. 13:1999;289-302
    • (1999) J. Biomol. NMR , vol.13 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 22
    • 2142654882 scopus 로고    scopus 로고
    • Characterization of iron binding in IscA, an ancient iron sulfur cluster assembly protein
    • Ding H., Clark R.J. Characterization of iron binding in IscA, an ancient iron sulfur cluster assembly protein. Biochem. J. 379:2004;433-440
    • (2004) Biochem. J. , vol.379 , pp. 433-440
    • Ding, H.1    Clark, R.J.2
  • 23
    • 4444317589 scopus 로고    scopus 로고
    • IscA mediates iron delivery for assembly of iron-sulfur clusters in IscU under the limited "free" iron conditions
    • Ding H., Clark R.J., Ding B. IscA mediates iron delivery for assembly of iron-sulfur clusters in IscU under the limited "free" iron conditions. J. Biol. Chem. 279:2004;37499-37504
    • (2004) J. Biol. Chem. , vol.279 , pp. 37499-37504
    • Ding, H.1    Clark, R.J.2    Ding, B.3
  • 24
    • 0032800601 scopus 로고    scopus 로고
    • Low iron concentration and aconitase deficiency in a yeast frataxin homologue deficient strain
    • Foury F. Low iron concentration and aconitase deficiency in a yeast frataxin homologue deficient strain. FEBS Lett. 6:1999;281-284
    • (1999) FEBS Lett. , vol.6 , pp. 281-284
    • Foury, F.1
  • 25
    • 0036670725 scopus 로고    scopus 로고
    • Biosynthesis of iron-sulphur clusters is a complex and highly conserved process
    • Frazzon J., Fick J.R., Dean D.R. Biosynthesis of iron-sulphur clusters is a complex and highly conserved process. Biochem. Soc. Trans. 30:2002;680-685
    • (2002) Biochem. Soc. Trans. , vol.30 , pp. 680-685
    • Frazzon, J.1    Fick, J.R.2    Dean, D.R.3
  • 26
    • 0033986734 scopus 로고    scopus 로고
    • The dodecameric ferritin from Listeria innocua contains a novel intersubunit iron-binding site
    • Ilari A., Stefanini S., Chiancone E., Tsernoglou D. The dodecameric ferritin from Listeria innocua contains a novel intersubunit iron-binding site. Nat. Struct. Biol. 7:2000;38-43
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 38-43
    • Ilari, A.1    Stefanini, S.2    Chiancone, E.3    Tsernoglou, D.4
  • 27
    • 0141623560 scopus 로고    scopus 로고
    • An interaction between frataxin and Isu1/Nfs1 that is crucial for Fe/S cluster synthesis on Isu1
    • Gerber J., Muhlenhoff U., Lill R. An interaction between frataxin and Isu1/Nfs1 that is crucial for Fe/S cluster synthesis on Isu1. EMBO Rep. 9:2003;906-911
    • (2003) EMBO Rep. , vol.9 , pp. 906-911
    • Gerber, J.1    Muhlenhoff, U.2    Lill, R.3
  • 28
    • 0030296878 scopus 로고    scopus 로고
    • Friedreich's ataxia protein: Phylogenetic evidence for mitochondrial dysfunction
    • Gibson T.J., Koonin E.V., Musco G., Pastore A., Bork P. Friedreich's ataxia protein. phylogenetic evidence for mitochondrial dysfunction Trends Neurosci. 19:1996;465-468
    • (1996) Trends Neurosci. , vol.19 , pp. 465-468
    • Gibson, T.J.1    Koonin, E.V.2    Musco, G.3    Pastore, A.4    Bork, P.5
  • 30
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for NMR structure calculation with the new program Dyana
    • Güntert P., Mumenthaler C., Wüthrich K. Torsion angle dynamics for NMR structure calculation with the new program Dyana. J. Mol. Biol. 273:1997;283-298
    • (1997) J. Mol. Biol. , vol.273 , pp. 283-298
    • Güntert, P.1    Mumenthaler, C.2    Wüthrich, K.3
  • 31
    • 0030608152 scopus 로고    scopus 로고
    • The ferritins: Molecular properties, iron storage function and cellular regulation
    • Harrison P.M., Arosio P. The ferritins. molecular properties, iron storage function and cellular regulation Biochim. Biophys. Acta. 1275:1996;161-203
    • (1996) Biochim. Biophys. Acta , vol.1275 , pp. 161-203
    • Harrison, P.M.1    Arosio, P.2
  • 32
    • 0035504444 scopus 로고    scopus 로고
    • The phylogenetic distribution of frataxin indicates a role in iron-sulfur cluster protein assembly
    • Huynen M.A., Snel B., Bork P., Gibson T.J. The phylogenetic distribution of frataxin indicates a role in iron-sulfur cluster protein assembly. Hum. Mol. Genet. 10:2001;2463-2468
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 2463-2468
    • Huynen, M.A.1    Snel, B.2    Bork, P.3    Gibson, T.J.4
  • 33
    • 0030813487 scopus 로고    scopus 로고
    • Studies of human, mouse and yeast homologues indicate a mitochondrial function for frataxin
    • Koutnikova H., Campuzano V., Foury F., Dolle P., Cazzalini O., Koenig M. Studies of human, mouse and yeast homologues indicate a mitochondrial function for frataxin. Nat. Genet. 16:1997;345-351
    • (1997) Nat. Genet. , vol.16 , pp. 345-351
    • Koutnikova, H.1    Campuzano, V.2    Foury, F.3    Dolle, P.4    Cazzalini, O.5    Koenig, M.6
  • 34
    • 0029881007 scopus 로고    scopus 로고
    • Molmol: A program for display and analysis of macromolecular structures
    • Koradi R., Billeter M., Wüthrich K. Molmol. a program for display and analysis of macromolecular structures J. Mol. Graph. 14:1996;51-55
    • (1996) J. Mol. Graph. , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 35
  • 37
    • 0019074845 scopus 로고
    • Strategies for the uses of lanthanide NMR shift probes in the determination of protein structure in solution. Application to the EF-calcium binding site of carp parvalbumin
    • Lee L., Sykes B.D. Strategies for the uses of lanthanide NMR shift probes in the determination of protein structure in solution. Application to the EF-calcium binding site of carp parvalbumin. Biophys. J. 32:1980;193-210
    • (1980) Biophys. J. , vol.32 , pp. 193-210
    • Lee, L.1    Sykes, B.D.2
  • 38
    • 0035970292 scopus 로고    scopus 로고
    • The mitochondrial proteins Ssq1 and Jac1 are required for the assembly of iron sulfur clusters in mitochondria
    • Lutz T., Westermann B., Neupert W., Herrmann J.M. The mitochondrial proteins Ssq1 and Jac1 are required for the assembly of iron sulfur clusters in mitochondria. J. Mol. Biol. 307:2001;815-825
    • (2001) J. Mol. Biol. , vol.307 , pp. 815-825
    • Lutz, T.1    Westermann, B.2    Neupert, W.3    Herrmann, J.M.4
  • 39
    • 0141737067 scopus 로고    scopus 로고
    • Components involved in assembly and dislocation of iron-sulfur clusters on the scaffold protein Isu1p
    • Muhlenhoff U., Gerber J., Richhardt N., Lill R. Components involved in assembly and dislocation of iron-sulfur clusters on the scaffold protein Isu1p. EMBO J. 22:2003;4815-4825
    • (2003) EMBO J. , vol.22 , pp. 4815-4825
    • Muhlenhoff, U.1    Gerber, J.2    Richhardt, N.3    Lill, R.4
  • 40
    • 0034661480 scopus 로고    scopus 로고
    • A structural understanding of genetic diseases: The solution structure of frataxin, the protein responsible for Friedreich Ataxia
    • Musco G., Stier G., Kolmerer B., Adinolfi S., Martin S., Frenkiel T., Gibson T., Pastore A. A structural understanding of genetic diseases. The solution structure of frataxin, the protein responsible for Friedreich Ataxia Structure. 8:2000;695-707
    • (2000) Structure , vol.8 , pp. 695-707
    • Musco, G.1    Stier, G.2    Kolmerer, B.3    Adinolfi, S.4    Martin, S.5    Frenkiel, T.6    Gibson, T.7    Pastore, A.8
  • 43
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A., Sharp K., Honig B. Protein folding and association. insights from the interfacial and thermodynamic properties of hydrocarbons Proteins. 11:1991;281-296
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.2    Honig, B.3
  • 44
    • 0032863136 scopus 로고    scopus 로고
    • Molecular pathogenesis of Friedreich ataxia
    • Pandolfo M. Molecular pathogenesis of Friedreich ataxia. Arch. Neurol. 56:1999;1201-1208
    • (1999) Arch. Neurol. , vol.56 , pp. 1201-1208
    • Pandolfo, M.1
  • 45
    • 0037064027 scopus 로고    scopus 로고
    • The ferroxidase activity of yeast frataxin
    • Park S., Gakh O., Mooney S.M., Isaya G. The ferroxidase activity of yeast frataxin. J. Biol. Chem. 277:2002;38589-38595
    • (2002) J. Biol. Chem. , vol.277 , pp. 38589-38595
    • Park, S.1    Gakh, O.2    Mooney, S.M.3    Isaya, G.4
  • 46
    • 0035874476 scopus 로고    scopus 로고
    • Subcellular distribution of chelatable iron: A laser scanning microscopic study in isolated hepatocytes and liver endothelial cell
    • Petrat F., de Groot H., Rauen U. Subcellular distribution of chelatable iron. a laser scanning microscopic study in isolated hepatocytes and liver endothelial cell Biochem. J. 356:2001;61-69
    • (2001) Biochem. J. , vol.356 , pp. 61-69
    • Petrat, F.1    De Groot, H.2    Rauen, U.3
  • 47
    • 1642573170 scopus 로고    scopus 로고
    • Mitochondrial functional interactions between frataxin and Isu1p, the iron-sulfur cluster scaffold protein, in Saccharomyces cerevisiae
    • Ramazzotti A., Vanmansart V., Foury F. Mitochondrial functional interactions between frataxin and Isu1p, the iron-sulfur cluster scaffold protein, in Saccharomyces cerevisiae. FEBS Lett. 557:2004;215-220
    • (2004) FEBS Lett. , vol.557 , pp. 215-220
    • Ramazzotti, A.1    Vanmansart, V.2    Foury, F.3
  • 48
    • 0036219167 scopus 로고    scopus 로고
    • Improving the quality of protein structures derived by NMR spectroscopy
    • Spronk C.A., Linge J.P., Hilbers C.W., Vuister G.W. Improving the quality of protein structures derived by NMR spectroscopy. J. Biomol. NMR. 22:2002;281-289
    • (2002) J. Biomol. NMR , vol.22 , pp. 281-289
    • Spronk, C.A.1    Linge, J.P.2    Hilbers, C.W.3    Vuister, G.W.4
  • 49
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTALX windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson J.D., Gibson T.J., Plewniak F., Jeanmougin F., Higgins D.G. The CLUSTALX windows interface. flexible strategies for multiple sequence alignment aided by quality analysis tools Nucleic Acids Res. 25:1997;4876-4882
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 50
    • 0037613459 scopus 로고    scopus 로고
    • Iron-sulfur cluster biosynthesis. Characterization of frataxin as an iron donor for assembly of [2Fe-2S] clusters in ISU-type proteins
    • Yoon T., Cowan J.A. Iron-sulfur cluster biosynthesis. Characterization of frataxin as an iron donor for assembly of [2Fe-2S] clusters in ISU-type proteins. J. Am. Chem. Soc. 125:2003;6078-6084
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 6078-6084
    • Yoon, T.1    Cowan, J.A.2
  • 51
    • 2942744572 scopus 로고    scopus 로고
    • Frataxin mediated iron delivery to ferrochelatase in the final step of heme biosynthesis
    • Yoon T., Cowan J.A. Frataxin mediated iron delivery to ferrochelatase in the final step of heme biosynthesis. J. Biol. Chem. 279:2004;25943-25946
    • (2004) J. Biol. Chem. , vol.279 , pp. 25943-25946
    • Yoon, T.1    Cowan, J.A.2
  • 52
    • 0025398721 scopus 로고
    • What if: A molecular modeling and drug design program
    • Vriend G. What if. a molecular modeling and drug design program J. Mol. Graph. 8:1990;52-56
    • (1990) J. Mol. Graph. , vol.8 , pp. 52-56
    • Vriend, G.1
  • 53
    • 12044259775 scopus 로고
    • Quantitative J correlation-A new approach for measuring homonuclear 3 bond J(H(N)H(α) coupling constants in N-15 enriched proteins
    • Vuister G.W., Bax A. Quantitative J correlation-A new approach for measuring homonuclear 3 bond J(H(N)H(α) coupling constants in N-15 enriched proteins. J. Am. Chem. Soc. 115:1993;7772-7777
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 7772-7777
    • Vuister, G.W.1    Bax, A.2
  • 54
    • 0003122737 scopus 로고
    • The chemistry of lanthanide ions in solution and in biological systems
    • Williams R.J. The chemistry of lanthanide ions in solution and in biological systems. Struct. Bond. 50:1979;79-119
    • (1979) Struct. Bond. , vol.50 , pp. 79-119
    • Williams, R.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.