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Volumn 290, Issue 50, 2015, Pages 29717-29731

Functional dynamics revealed by the structure of the SufBCD Complex, a novel ATP-binding cassette (ABC) protein that serves as a scaffold for iron-sulfur cluster biogenesis

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; BIOSYNTHESIS; CHROMOSOMES; ESCHERICHIA COLI; IRON; IRON COMPOUNDS; PROTEINS; SCAFFOLDS (BIOLOGY);

EID: 84949670314     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M115.680934     Document Type: Article
Times cited : (57)

References (61)
  • 1
    • 0026621245 scopus 로고
    • ABC transporters: From microorganisms to man
    • Higgins, C. F. (1992) ABC transporters: from microorganisms to man. Annu. Rev. Cell Biol. 8, 67-113
    • (1992) Annu. Rev. Cell Biol. , vol.8 , pp. 67-113
    • Higgins, C.F.1
  • 2
    • 0036909285 scopus 로고    scopus 로고
    • Structure and mechanism ofABCtransporters
    • Schmitt, L., and Tampé, R. (2002) Structure and mechanism ofABCtransporters. Curr. Opin. Struct. Biol. 12, 754-760
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 754-760
    • Schmitt, L.1    Tampé, R.2
  • 4
    • 0037398027 scopus 로고    scopus 로고
    • Rad50/SMC proteins and ABC transporters: Unifying concepts from high-resolution structures
    • Hopfner, K. P., and Tainer, J. A. (2003) Rad50/SMC proteins and ABC transporters: unifying concepts from high-resolution structures. Curr. Opin. Struct. Biol. 13, 249-255
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 249-255
    • Hopfner, K.P.1    Tainer, J.A.2
  • 5
    • 0032698874 scopus 로고    scopus 로고
    • ABC-ATPases, adaptable energy generators fuelling transmembrane movement of a variety of molecules in organisms from bacteria to humans
    • Holland, I. B., and Blight, M. A. (1999) ABC-ATPases, adaptable energy generators fuelling transmembrane movement of a variety of molecules in organisms from bacteria to humans. J. Mol. Biol. 293, 381-399
    • (1999) J. Mol. Biol. , vol.293 , pp. 381-399
    • Holland, I.B.1    Blight, M.A.2
  • 6
    • 20544465434 scopus 로고    scopus 로고
    • SMC proteins and chromosome mechanics: From bacteria to humans
    • Hirano, T. (2005) SMC proteins and chromosome mechanics: from bacteria to humans. Philos. Trans. R. Soc. Lond. B Biol. Sci. 360, 507-514
    • (2005) Philos. Trans. R. Soc. Lond. B Biol. Sci. , vol.360 , pp. 507-514
    • Hirano, T.1
  • 7
    • 0034705293 scopus 로고    scopus 로고
    • Structural biology of Rad50 ATPase: ATPdriven conformational control inDNAdouble-strand break repair and the ABC-ATPase superfamily
    • Hopfner, K. P., Karcher, A., Shin, D. S., Craig, L., Arthur, L. M., Carney, J. P., and Tainer, J. A. (2000) Structural biology of Rad50 ATPase: ATPdriven conformational control inDNAdouble-strand break repair and the ABC-ATPase superfamily. Cell 101, 789-800
    • (2000) Cell , vol.101 , pp. 789-800
    • Hopfner, K.P.1    Karcher, A.2    Shin, D.S.3    Craig, L.4    Arthur, L.M.5    Carney, J.P.6    Tainer, J.A.7
  • 8
    • 0035119398 scopus 로고    scopus 로고
    • SMC proteins in bacteria: Condensation motors for chromosome segregation?
    • Graumann, P. L. (2001) SMC proteins in bacteria: condensation motors for chromosome segregation? Biochimie 83, 53-59
    • (2001) Biochimie , vol.83 , pp. 53-59
    • Graumann, P.L.1
  • 9
    • 21444455377 scopus 로고    scopus 로고
    • Biogenesis of iron-sulfur proteins in plants
    • Balk, J., and Lobréaux, S. (2005) Biogenesis of iron-sulfur proteins in plants. Trends Plant Sci. 10, 324-331
    • (2005) Trends Plant Sci. , vol.10 , pp. 324-331
    • Balk, J.1    Lobréaux, S.2
  • 10
    • 0037047411 scopus 로고    scopus 로고
    • A third bacterial system for the assembly of iron-sulfur clusters with homologs in archaea and plastids
    • Takahashi, Y., and Tokumoto, U. (2002) A third bacterial system for the assembly of iron-sulfur clusters with homologs in archaea and plastids. J. Biol. Chem. 277, 28380-28383
    • (2002) J. Biol. Chem. , vol.277 , pp. 28380-28383
    • Takahashi, Y.1    Tokumoto, U.2
  • 11
    • 0030868605 scopus 로고    scopus 로고
    • Iron-sulfur clusters: Nature's modular, multipurpose structures
    • Beinert, H., Holm, R. H., and Münck, E. (1997) Iron-sulfur clusters: nature's modular, multipurpose structures. Science 277, 653-659
    • (1997) Science , vol.277 , pp. 653-659
    • Beinert, H.1    Holm, R.H.2    Münck, E.3
  • 12
    • 0038670302 scopus 로고    scopus 로고
    • The interface between the biological and inorganic worlds: Iron-sulfur metalloclusters
    • Rees, D. C., and Howard, J. B. (2003) The interface between the biological and inorganic worlds: iron-sulfur metalloclusters. Science 300, 929-931
    • (2003) Science , vol.300 , pp. 929-931
    • Rees, D.C.1    Howard, J.B.2
  • 13
    • 0141532194 scopus 로고    scopus 로고
    • Biogenesis of Fe-S cluster by the bacterial Suf system: SufS and SufE form a new type of cysteine desulfurase
    • Loiseau, L., Ollagnier-de-Choudens, S., Nachin, L., Fontecave, M., and Barras, F. (2003) Biogenesis of Fe-S cluster by the bacterial Suf system: SufS and SufE form a new type of cysteine desulfurase. J. Biol. Chem. 278, 38352-38359
    • (2003) J. Biol. Chem. , vol.278 , pp. 38352-38359
    • Loiseau, L.1    Ollagnier-De-Choudens, S.2    Nachin, L.3    Fontecave, M.4    Barras, F.5
  • 15
    • 69949162828 scopus 로고    scopus 로고
    • Native Escherichia coli SufA, coexpressed with SufBCDSE, purifies as a [2Fe-2S] protein and acts as an Fe-S transporter to Fe-S target enzymes
    • Gupta, V., Sendra, M., Naik, S. G., Chahal, H. K., Huynh, B. H., Outten, F. W., Fontecave, M., and Ollagnier de Choudens, S. (2009) Native Escherichia coli SufA, coexpressed with SufBCDSE, purifies as a [2Fe-2S] protein and acts as an Fe-S transporter to Fe-S target enzymes. J. Am. Chem. Soc. 131, 6149-6153
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 6149-6153
    • Gupta, V.1    Sendra, M.2    Naik, S.G.3    Chahal, H.K.4    Huynh, B.H.5    Outten, F.W.6    Fontecave, M.7    Ollagnier De Choudens, S.8
  • 16
    • 4644354002 scopus 로고    scopus 로고
    • Interchangeability and distinct properties of bacterial Fe-S cluster assembly systems: Functional replacement of the isc and suf operons in Escherichia coli with the nifSU-like operon from Helicobacter pylori
    • Tokumoto, U., Kitamura, S., Fukuyama, K., and Takahashi, Y. (2004) Interchangeability and distinct properties of bacterial Fe-S cluster assembly systems: functional replacement of the isc and suf operons in Escherichia coli with the nifSU-like operon from Helicobacter pylori. J. Biochem. 136, 199-209
    • (2004) J. Biochem. , vol.136 , pp. 199-209
    • Tokumoto, U.1    Kitamura, S.2    Fukuyama, K.3    Takahashi, Y.4
  • 17
    • 2442567822 scopus 로고    scopus 로고
    • A suf operon requirement for Fe-S cluster assembly during iron starvation in Escherichia coli
    • Outten, F. W., Djaman, O., and Storz, G. (2004) A suf operon requirement for Fe-S cluster assembly during iron starvation in Escherichia coli. Mol. Microbiol. 52, 861-872
    • (2004) Mol. Microbiol. , vol.52 , pp. 861-872
    • Outten, F.W.1    Djaman, O.2    Storz, G.3
  • 18
    • 78049288246 scopus 로고    scopus 로고
    • SufD and SufC ATPase activity are required for iron acquisition during in vivo Fe-S cluster formation on SufB
    • Saini, A., Mapolelo, D. T., Chahal, H. K., Johnson, M. K., and Outten, F. W. (2010) SufD and SufC ATPase activity are required for iron acquisition during in vivo Fe-S cluster formation on SufB. Biochemistry 49, 9402-9412
    • (2010) Biochemistry , vol.49 , pp. 9402-9412
    • Saini, A.1    Mapolelo, D.T.2    Chahal, H.K.3    Johnson, M.K.4    Outten, F.W.5
  • 19
    • 46449094234 scopus 로고    scopus 로고
    • Hydrodynamic characterization of the SufBC and SufCD complexes and their interaction with fluorescent adenosine nucleotides
    • Petrovic, A., Davis, C. T., Rangachari, K., Clough, B., Wilson, R. J., and Eccleston, J. F. (2008) Hydrodynamic characterization of the SufBC and SufCD complexes and their interaction with fluorescent adenosine nucleotides. Protein Sci. 17, 1264-1274
    • (2008) Protein Sci. , vol.17 , pp. 1264-1274
    • Petrovic, A.1    Davis, C.T.2    Rangachari, K.3    Clough, B.4    Wilson, R.J.5    Eccleston, J.F.6
  • 21
    • 0037415722 scopus 로고    scopus 로고
    • SufC: An unorthodox cytoplasmic ABC/ATPase required for [Fe-S] biogenesis under oxidative stress
    • Nachin, L., Loiseau, L., Expert, D., and Barras, F. (2003) SufC: an unorthodox cytoplasmic ABC/ATPase required for [Fe-S] biogenesis under oxidative stress. EMBO J. 22, 427-437
    • (2003) EMBO J. , vol.22 , pp. 427-437
    • Nachin, L.1    Loiseau, L.2    Expert, D.3    Barras, F.4
  • 22
    • 0242664733 scopus 로고    scopus 로고
    • The SufE protein and the SufBCD complex enhance SufS cysteine desulfurase activity as part of a sulfur transfer pathway for Fe-S cluster assembly in Escherichia coli
    • Outten, F. W., Wood, M. J., Munoz, F. M., and Storz, G. (2003) The SufE protein and the SufBCD complex enhance SufS cysteine desulfurase activity as part of a sulfur transfer pathway for Fe-S cluster assembly in Escherichia coli. J. Biol. Chem. 278, 45713-45719
    • (2003) J. Biol. Chem. , vol.278 , pp. 45713-45719
    • Outten, F.W.1    Wood, M.J.2    Munoz, F.M.3    Storz, G.4
  • 23
    • 70449455583 scopus 로고    scopus 로고
    • The SufBCD Fe-S scaffold complex interacts with SufA for Fe-S cluster transfer
    • Chahal, H. K., Dai, Y., Saini, A., Ayala-Castro, C., and Outten, F. W. (2009) The SufBCD Fe-S scaffold complex interacts with SufA for Fe-S cluster transfer. Biochemistry 48, 10644-10653
    • (2009) Biochemistry , vol.48 , pp. 10644-10653
    • Chahal, H.K.1    Dai, Y.2    Saini, A.3    Ayala-Castro, C.4    Outten, F.W.5
  • 26
    • 0037084037 scopus 로고    scopus 로고
    • The ABCs of SMC proteins: Two-armed ATPases for chromosome condensation, cohesion, and repair
    • Hirano, T. (2002) The ABCs of SMC proteins: two-armed ATPases for chromosome condensation, cohesion, and repair. Genes Dev. 16, 399-414
    • (2002) Genes Dev. , vol.16 , pp. 399-414
    • Hirano, T.1
  • 27
    • 0031059866 scopus 로고    scopus 로고
    • Processing of x-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., and Minor, W. (1997) Processing of x-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 30
    • 0030039296 scopus 로고    scopus 로고
    • PROMOTIF: A program to identify and analyze structural motifs in proteins
    • Hutchinson, E. G., and Thornton, J. M. (1996) PROMOTIF: a program to identify and analyze structural motifs in proteins. Protein Sci. 5, 212-220
    • (1996) Protein Sci. , vol.5 , pp. 212-220
    • Hutchinson, E.G.1    Thornton, J.M.2
  • 31
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., MacArthur, M. W., Moss, D. S., and Thornton, J. M. (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 32
    • 0030501419 scopus 로고    scopus 로고
    • Use of non-crystallographic symmetry in protein structure refinement
    • Kleywegt, G. (1996) Use of non-crystallographic symmetry in protein structure refinement. Acta Crystallogr. D 52, 842-857
    • (1996) Acta Crystallogr. D , vol.52 , pp. 842-857
    • Kleywegt, G.1
  • 36
    • 58049204808 scopus 로고    scopus 로고
    • SPIDER image processing for single-particle reconstruction of biological macromolecules from electron micrographs
    • Shaikh, T. R., Gao, H., Baxter, W. T., Asturias, F. J., Boisset, N., Leith, A., and Frank, J. (2008) SPIDER image processing for single-particle reconstruction of biological macromolecules from electron micrographs. Nat. Protoc. 3, 1941-1974
    • (2008) Nat. Protoc. , vol.3 , pp. 1941-1974
    • Shaikh, T.R.1    Gao, H.2    Baxter, W.T.3    Asturias, F.J.4    Boisset, N.5    Leith, A.6    Frank, J.7
  • 37
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: Semiautomated software for high-resolution single-particle reconstructions
    • Ludtke, S. J., Baldwin, P. R., and Chiu, W. (1999) EMAN: semiautomated software for high-resolution single-particle reconstructions. J. Struct. Biol. 128, 82-97
    • (1999) J. Struct. Biol. , vol.128 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 39
    • 0029185933 scopus 로고
    • CRYSOL: A program to evaluate x-ray solution scattering of biological macromolecules from atomic coordinates
    • Svergun, D., Barberato, C., and Koch, M. H. J. (1995) CRYSOL: a program to evaluate x-ray solution scattering of biological macromolecules from atomic coordinates. J. Appl. Crystallogr. 28, 768-773
    • (1995) J. Appl. Crystallogr. , vol.28 , pp. 768-773
    • Svergun, D.1    Barberato, C.2    Koch, M.H.J.3
  • 40
    • 62649139615 scopus 로고    scopus 로고
    • DAMMIF, a program for rapid abinitio shape determination in small-angle scattering
    • Franke, D., and Svergun, D. I. (2009) DAMMIF, a program for rapid abinitio shape determination in small-angle scattering. J. Appl. Crystallogr. 42, 342-346
    • (2009) J. Appl. Crystallogr. , vol.42 , pp. 342-346
    • Franke, D.1    Svergun, D.I.2
  • 41
    • 0037701585 scopus 로고    scopus 로고
    • Uniqueness of ab initio shape determination in small-angle scattering
    • Volkov, V. V., and Svergun, D. I. (2003) Uniqueness of ab initio shape determination in small-angle scattering. J. Appl. Crystallogr. 36, 860-864
    • (2003) J. Appl. Crystallogr. , vol.36 , pp. 860-864
    • Volkov, V.V.1    Svergun, D.I.2
  • 42
    • 0032868231 scopus 로고    scopus 로고
    • Hyperproduction of recombinant ferredoxins in Escherichia coli by coexpression of the ORF1-ORF2-iscS-iscU-iscA-hscB-hscA-fdx-ORF3 gene cluster
    • Nakamura, M., Saeki, K., and Takahashi, Y. (1999) Hyperproduction of recombinant ferredoxins in Escherichia coli by coexpression of the ORF1-ORF2-iscS-iscU-iscA-hscB-hscA-fdx-ORF3 gene cluster. J. Biochem. 126, 10-18
    • (1999) J. Biochem. , vol.126 , pp. 10-18
    • Nakamura, M.1    Saeki, K.2    Takahashi, Y.3
  • 43
    • 0028793123 scopus 로고
    • Four new derivatives of the broadhost-range cloning vector pBBR1MCS, carrying different antibiotic-resistance cassettes
    • Kovach, M. E., Elzer, P. H., Hill, D. S., Robertson, G. T., Farris, M. A., Roop, R. M., 2nd, and Peterson, K. M. (1995) Four new derivatives of the broadhost-range cloning vector pBBR1MCS, carrying different antibiotic-resistance cassettes. Gene 166, 175-176
    • (1995) Gene , vol.166 , pp. 175-176
    • Kovach, M.E.1    Elzer, P.H.2    Hill, D.S.3    Robertson, G.T.4    Farris, M.A.5    Roop, R.M.6    Peterson, I.I.K.M.7
  • 46
    • 0029853148 scopus 로고    scopus 로고
    • WWW-query: An on-line retrieval system for biological sequence banks
    • Perrière, G., and Gouy, M. (1996) WWW-query: an on-line retrieval system for biological sequence banks. Biochimie 78, 364-369
    • (1996) Biochimie , vol.78 , pp. 364-369
    • Perrière, G.1    Gouy, M.2
  • 47
    • 84904790793 scopus 로고    scopus 로고
    • Deciphering key features in protein structures with the new ENDscript server
    • Robert, X., and Gouet, P. (2014) Deciphering key features in protein structures with the new ENDscript server. Nucleic Acids Res. 42, W320-W324
    • (2014) Nucleic Acids Res. , vol.42 , pp. W320-W324
    • Robert, X.1    Gouet, P.2
  • 51
    • 29344433036 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli SufC, an ABC-type ATPase component of the SUF iron-sulfur cluster assembly machinery
    • Kitaoka, S., Wada, K., Hasegawa, Y., Minami, Y., Fukuyama, K., and Takahashi, Y. (2006) Crystal structure of Escherichia coli SufC, an ABC-type ATPase component of the SUF iron-sulfur cluster assembly machinery. FEBS Lett. 580, 137-143
    • (2006) FEBS Lett. , vol.580 , pp. 137-143
    • Kitaoka, S.1    Wada, K.2    Hasegawa, Y.3    Minami, Y.4    Fukuyama, K.5    Takahashi, Y.6
  • 52
    • 0036342413 scopus 로고    scopus 로고
    • ATP binding to the motor domain from anABC transporter drives formation of a nucleotide sandwich dimer
    • Smith, P. C., Karpowich, N., Millen, L., Moody, J. E., Rosen, J., Thomas, P. J., and Hunt, J. F. (2002) ATP binding to the motor domain from anABC transporter drives formation of a nucleotide sandwich dimer. Mol. Cell 10, 139-149
    • (2002) Mol. Cell , vol.10 , pp. 139-149
    • Smith, P.C.1    Karpowich, N.2    Millen, L.3    Moody, J.E.4    Rosen, J.5    Thomas, P.J.6    Hunt, J.F.7
  • 53
    • 21244454073 scopus 로고    scopus 로고
    • H662 is the linchpin of ATP hydrolysis in the nucleotide-binding domain of the ABC transporter HlyB
    • Zaitseva, J., Jenewein, S., Jumpertz, T., Holland, I. B., and Schmitt, L. (2005) H662 is the linchpin of ATP hydrolysis in the nucleotide-binding domain of the ABC transporter HlyB. EMBO J. 24, 1901-1910
    • (2005) EMBO J. , vol.24 , pp. 1901-1910
    • Zaitseva, J.1    Jenewein, S.2    Jumpertz, T.3    Holland, I.B.4    Schmitt, L.5
  • 54
    • 0032542358 scopus 로고    scopus 로고
    • Crystal structure of the ATP-binding subunit of an ABC transporter
    • Hung, L. W., Wang, I. X., Nikaido, K., Liu, P. Q., Ames, G. F., and Kim, S. H. (1998) Crystal structure of the ATP-binding subunit of an ABC transporter. Nature 396, 703-707
    • (1998) Nature , vol.396 , pp. 703-707
    • Hung, L.W.1    Wang, I.X.2    Nikaido, K.3    Liu, P.Q.4    Ames, G.F.5    Kim, S.H.6
  • 55
    • 44649133131 scopus 로고    scopus 로고
    • Extrinsic fluorescent dyes as tools for protein characterization
    • Hawe, A., Sutter, M., and Jiskoot, W. (2008) Extrinsic fluorescent dyes as tools for protein characterization. Pharm. Res. 25, 1487-1499
    • (2008) Pharm. Res. , vol.25 , pp. 1487-1499
    • Hawe, A.1    Sutter, M.2    Jiskoot, W.3
  • 56
    • 0020658252 scopus 로고
    • N-(7-Dimethylamino-4-methylcoumarinyl)-maleimide (DACM): An alternative label for fluorescence tracing
    • Namihisa, T., Saifuku, K., Ishii, H., Watanabe, S., and Sekine, T. (1983) N-(7-Dimethylamino-4-methylcoumarinyl)-maleimide (DACM): an alternative label for fluorescence tracing. J. Immunol. Methods 56, 125-134
    • (1983) J. Immunol. Methods , vol.56 , pp. 125-134
    • Namihisa, T.1    Saifuku, K.2    Ishii, H.3    Watanabe, S.4    Sekine, T.5
  • 57
    • 0018800026 scopus 로고
    • Preparation and partial characterization of iron-sulfur, iron-selenium, and iron-tellurium complexes of bovine serum albumin
    • Arakawa, S., and Kimura, T. (1979) Preparation and partial characterization of iron-sulfur, iron-selenium, and iron-tellurium complexes of bovine serum albumin. Biochim. Biophys. Acta 580, 382-391
    • (1979) Biochim. Biophys. Acta , vol.580 , pp. 382-391
    • Arakawa, S.1    Kimura, T.2
  • 58
    • 84884678911 scopus 로고    scopus 로고
    • The suf iron-sulfur cluster synthesis pathway is required for apicoplast maintenance in malaria parasites
    • Gisselberg, J. E., Dellibovi-Ragheb, T. A., Matthews, K. A., Bosch, G., and Prigge, S. T. (2013) The suf iron-sulfur cluster synthesis pathway is required for apicoplast maintenance in malaria parasites. PLoS Pathog. 9, e1003655
    • (2013) PLoS Pathog. , vol.9
    • Gisselberg, J.E.1    Dellibovi-Ragheb, T.A.2    Matthews, K.A.3    Bosch, G.4    Prigge, S.T.5
  • 59
    • 20744446399 scopus 로고    scopus 로고
    • Structure, function, and formation of biological iron-sulfur clusters
    • Johnson, D. C., Dean, D. R., Smith, A. D., and Johnson, M. K. (2005) Structure, function, and formation of biological iron-sulfur clusters. Annu. Rev. Biochem. 74, 247-281
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 247-281
    • Johnson, D.C.1    Dean, D.R.2    Smith, A.D.3    Johnson, M.K.4
  • 60
    • 68949128587 scopus 로고    scopus 로고
    • Function and biogenesis of iron-sulphur proteins
    • Lill, R. (2009) Function and biogenesis of iron-sulphur proteins. Nature 460, 831-838
    • (2009) Nature , vol.460 , pp. 831-838
    • Lill, R.1
  • 61
    • 52049096425 scopus 로고    scopus 로고
    • The asymmetric trimeric architecture of [2Fe-2S] IscU: Implications for its scaffolding during iron-sulfur cluster biosynthesis
    • Shimomura, Y., Wada, K., Fukuyama, K., and Takahashi, Y. (2008) The asymmetric trimeric architecture of [2Fe-2S] IscU: implications for its scaffolding during iron-sulfur cluster biosynthesis. J. Mol. Biol. 383, 133-143
    • (2008) J. Mol. Biol. , vol.383 , pp. 133-143
    • Shimomura, Y.1    Wada, K.2    Fukuyama, K.3    Takahashi, Y.4


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