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Volumn 288, Issue 38, 2013, Pages 27172-27180

Structural changes during cysteine desulfurase CsdA and sulfur acceptor CsdE interactions provide insight into the trans-persulfuration

Author keywords

[No Author keywords available]

Indexed keywords

BINDING MODES; BIOLOGICAL PROCESS; CONFORMATIONAL FLEXIBILITY; CYSTEINE DESULFURASE; CYSTEINE RESIDUES; SULFUR TRANSFER;

EID: 84884574069     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.480277     Document Type: Article
Times cited : (42)

References (36)
  • 1
    • 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
  • 2
    • 44549087696 scopus 로고    scopus 로고
    • Iron-sulfur cluster biosynthesis in bacteria, mechanisms of cluster assembly and transfer
    • Fontecave, M., and Ollagnier-de-Choudens, S. (2008) Iron-sulfur cluster biosynthesis in bacteria, mechanisms of cluster assembly and transfer. Arch. Biochem. Biophys. 474, 226-237
    • (2008) Arch. Biochem. Biophys. , vol.474 , pp. 226-237
    • Fontecave, M.1    Ollagnier-De-Choudens, S.2
  • 3
    • 77952813340 scopus 로고    scopus 로고
    • Building Fe-S proteins: Bacterial strategies
    • Py, B., and Barras, F. (2010) Building Fe-S proteins: bacterial strategies. Nat. Rev. Microbiol. 8, 436-446
    • (2010) Nat. Rev. Microbiol. , vol.8 , pp. 436-446
    • Py, B.1    Barras, F.2
  • 4
    • 14744294785 scopus 로고    scopus 로고
    • Iron-sulfur-protein biogenesis in eukaryotes
    • Lill, R., and Mühlenhoff, U. (2005) Iron-sulfur-protein biogenesis in eukaryotes. Trends Biochem. Sci. 30, 133-141
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 133-141
    • Lill, R.1    Mühlenhoff, U.2
  • 5
    • 0027450059 scopus 로고
    • Cysteine desulfurase activity indicates a role for NIFS in metallocluster biosynthesis
    • Zheng, L., White, R. H., Cash, V. L., Jack, R. F., and Dean, D. R. (1993) Cysteine desulfurase activity indicates a role for NIFS in metallocluster biosynthesis. Proc. Natl. Acad. Sci. U. S. A. 90, 2754-2758
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 2754-2758
    • Zheng, L.1    White, R.H.2    Cash, V.L.3    Jack, R.F.4    Dean, D.R.5
  • 6
    • 0030963659 scopus 로고    scopus 로고
    • Cysteine sulfinate desulfinase, a NIFS-like protein of Escherichia coli with selenocysteine lyase and cysteine desulfurase activities. Gene cloning, purification, and characterization of a novel pyridoxal enzyme
    • Mihara, H., Kurihara, T., Yoshimura, T., Soda, K., and Esaki, N. (1997) Cysteine sulfinate desulfinase, a NIFS-like protein of Escherichia coli with selenocysteine lyase and cysteine desulfurase activities. Gene cloning, purification, and characterization of a novel pyridoxal enzyme. J. Biol. Chem. 272, 22417-22424
    • (1997) J. Biol. Chem. , vol.272 , pp. 22417-22424
    • Mihara, H.1    Kurihara, T.2    Yoshimura, T.3    Soda, K.4    Esaki, N.5
  • 9
    • 33947540909 scopus 로고    scopus 로고
    • The SUF iron-sulfur cluster biosynthetic machinery: Sulfur transfer from the SUFS-SUFE complex to SUFA
    • Sendra, M., Ollagnier De Choudens, S., Lascoux, D., Sanakis, Y., and Fontecave, M. (2007) The SUF iron-sulfur cluster biosynthetic machinery: sulfur transfer from the SUFS-SUFE complex to SUFA. FEBS Lett. 581, 1362-1368
    • (2007) FEBS Lett. , vol.581 , pp. 1362-1368
    • Sendra, M.1    Ollagnier De Choudens, S.2    Lascoux, D.3    Sanakis, Y.4    Fontecave, M.5
  • 11
    • 0033591390 scopus 로고    scopus 로고
    • A nifS-like gene, csdB, encodes an Escherichia coli counterpart of mammalian selenocysteine lyase. Gene cloning, purification, characterization, and preliminary x-ray crystallographic studies
    • Mihara, H., Maeda, M., Fujii, T., Kurihara, T., Hata, Y., and Esaki, N. (1999) A nifS-like gene, csdB, encodes an Escherichia coli counterpart of mammalian selenocysteine lyase. Gene cloning, purification, characterization, and preliminary x-ray crystallographic studies. J. Biol. Chem. 274, 14768-14772
    • (1999) J. Biol. Chem. , vol.274 , pp. 14768-14772
    • Mihara, H.1    Maeda, M.2    Fujii, T.3    Kurihara, T.4    Hata, Y.5    Esaki, N.6
  • 12
    • 0034673177 scopus 로고    scopus 로고
    • Structure of an NifS homologue: X-ray structure analysis of CsdB, an Escherichia coli counterpart of mammalian selenocysteine lyase
    • Fujii, T., Maeda, M., Mihara, H., Kurihara, T., Esaki, N., and Hata, Y. (2000) Structure of an NifS homologue: x-ray structure analysis of CsdB, an Escherichia coli counterpart of mammalian selenocysteine lyase. Biochemistry 39, 1263-1273
    • (2000) Biochemistry , vol.39 , pp. 1263-1273
    • Fujii, T.1    Maeda, M.2    Mihara, H.3    Kurihara, T.4    Esaki, N.5    Hata, Y.6
  • 13
    • 0036303444 scopus 로고    scopus 로고
    • Analysis of the E coli NifS CsdB protein at 2.0Åreveals the structural basis for perselenide and persulfide intermediate formation
    • Lima, C. D. (2002) Analysis of the E. coli NifS CsdB protein at 2.0Åreveals the structural basis for perselenide and persulfide intermediate formation. J. Mol. Biol. 315, 1199-1208
    • (2002) J. Mol. Biol. , vol.315 , pp. 1199-1208
    • Lima, C.D.1
  • 14
    • 7444248431 scopus 로고    scopus 로고
    • The SufE sulfur acceptor protein contains a conserved core structure that mediates interdomain interactions in a variety of redox protein complexes
    • Goldsmith-Fischman, S., Kuzin, A., Edstrom, W. C., Benach, J., Shastry, R., Xiao, R., Acton, T. B., Honig, B., Montelione, G. T., and Hunt, J. F. (2004) The SufE sulfur acceptor protein contains a conserved core structure that mediates interdomain interactions in a variety of redox protein complexes. J. Mol. Biol. 344, 549-565
    • (2004) J. Mol. Biol. , vol.344 , pp. 549-565
    • Goldsmith-Fischman, S.1    Kuzin, A.2    Edstrom, W.C.3    Benach, J.4    Shastry, R.5    Xiao, R.6    Acton, T.B.7    Honig, B.8    Montelione, G.T.9    Hunt, J.F.10
  • 15
    • 21244464249 scopus 로고    scopus 로고
    • Analysis of the heteromeric CsdA-CsdE cysteine desulfurase, assisting Fe-S cluster biogenesis in Escherichia coli
    • Loiseau, L., Ollagnier-de Choudens, S., Lascoux, D., Forest, E., Fontecave, M., and Barras, F. (2005) Analysis of the heteromeric CsdA-CsdE cysteine desulfurase, assisting Fe-S cluster biogenesis in Escherichia coli. J. Biol. Chem. 280, 26760-26769
    • (2005) J. Biol. Chem. , vol.280 , pp. 26760-26769
    • Loiseau, L.1    Ollagnier-De Choudens, S.2    Lascoux, D.3    Forest, E.4    Fontecave, M.5    Barras, F.6
  • 16
    • 72049124821 scopus 로고    scopus 로고
    • The CsdA cysteine desulphurase promotes Fe/S biogenesis by recruiting Suf components and participates to a new sulphur transfer pathway by recruiting CsdL (ex-YgdL), a ubiquitin-modifyinglike protein
    • Trotter, V., Vinella, D., Loiseau, L., Ollagnier De Choudens, S., Fontecave, M., and Barras, F. (2009) The CsdA cysteine desulphurase promotes Fe/S biogenesis by recruiting Suf components and participates to a new sulphur transfer pathway by recruiting CsdL (ex-YgdL), a ubiquitin-modifyinglike protein. Mol. Microbiol. 74, 1527-1542
    • (2009) Mol. Microbiol. , vol.74 , pp. 1527-1542
    • Trotter, V.1    Vinella, D.2    Loiseau, L.3    Ollagnier De Choudens, S.4    Fontecave, M.5    Barras, F.6
  • 17
    • 22444449790 scopus 로고    scopus 로고
    • High-quality homology models derived from NMR and x-ray structures of E coli proteins YgdK and SufE suggest that all members of the YgdK/Suf E protein family are enhancers of cysteine desulfurases
    • Liu, G., Li, Z., Chiang, Y., Acton, T., Montelione, G. T., Murray, D., and Szyperski, T. (2005) High-quality homology models derived from NMR and x-ray structures of E. coli proteins YgdK and SufE suggest that all members of the YgdK/Suf E protein family are enhancers of cysteine desulfurases. Protein Sci. 14, 1597-1608
    • (2005) Protein Sci. , vol.14 , pp. 1597-1608
    • Liu, G.1    Li, Z.2    Chiang, Y.3    Acton, T.4    Montelione, G.T.5    Murray, D.6    Szyperski, T.7
  • 19
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill, S. C., and Von Hippel, P. H. (1989) Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182, 319-326
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 20
    • 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
  • 22
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An automated program for molecular replacement
    • Vagin, A., and Teplyakov, A. (1997) MOLREP: an automated program for molecular replacement. J. Appl. Crystallogr. 30, 1022-1025
    • (1997) J. Appl. Crystallogr. , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 23
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • Perrakis, A., Morris, R., and Lamzin, V. S. (1999) Automated protein model building combined with iterative structure refinement. Nat. Struct. Biol. 6, 458-463
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3
  • 24
  • 26
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel, E., and Henrick, K. (2007) Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 372, 774-797
    • (2007) J. Mol. Biol. , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 27
    • 0038351831 scopus 로고    scopus 로고
    • Crystal structure of IscS, a cysteine desulfurase from Escherichia coli
    • Cupp-Vickery, J. R., Urbina, H., and Vickery, L. E. (2003) Crystal structure of IscS, a cysteine desulfurase from Escherichia coli. J. Mol. Biol. 330, 1049-1059
    • (2003) J. Mol. Biol. , vol.330 , pp. 1049-1059
    • Cupp-Vickery, J.R.1    Urbina, H.2    Vickery, L.E.3
  • 28
    • 0034636007 scopus 로고    scopus 로고
    • Crystal structure of the cystine C-S lyase from synechocystis: Stabilization of cysteine persulfide for FES cluster biosynthesis
    • Clausen, T., Kaiser, J. T., Steegborn, C., Huber, R., and Kessler, D. (2000) Crystal structure of the cystine C-S lyase from synechocystis: stabilization of cysteine persulfide for FES cluster biosynthesis. Proc. Natl. Acad. Sci. U. S. A. 97, 3856-3861
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 3856-3861
    • Clausen, T.1    Kaiser, J.T.2    Steegborn, C.3    Huber, R.4    Kessler, D.5
  • 29
    • 0034708346 scopus 로고    scopus 로고
    • Crystal structure of a NifS-like protein from Thermotoga maritima: Implications for iron sulphur cluster assembly
    • Kaiser, J. T., Clausen, T., Bourenkow, G. P., Bartunik, H. D., Steinbacher, S., and Huber, R. (2000) Crystal structure of a NifS-like protein from Thermotoga maritima: implications for iron sulphur cluster assembly. J. Mol. Biol. 297, 451-464
    • (2000) J. Mol. Biol. , vol.297 , pp. 451-464
    • Kaiser, J.T.1    Clausen, T.2    Bourenkow, G.P.3    Bartunik, H.D.4    Steinbacher, S.5    Huber, R.6
  • 31
    • 0345303679 scopus 로고    scopus 로고
    • Mechanistic studies of the SufS-SufE cysteine desulfurase: Evidence for sulfur transfer from SufS to SufE
    • Ollagnier-de-Choudens, S., Lascoux, D., Loiseau, L., Barras, F., Forest, E., and Fontecave, M. (2003) Mechanistic studies of the SufS-SufE cysteine desulfurase: evidence for sulfur transfer from SufS to SufE. FEBS Lett. 555, 263-267
    • (2003) FEBS Lett. , vol.555 , pp. 263-267
    • Ollagnier-De-Choudens, S.1    Lascoux, D.2    Loiseau, L.3    Barras, F.4    Forest, E.5    Fontecave, M.6
  • 34
    • 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
  • 35
    • 0034711380 scopus 로고    scopus 로고
    • High precisionNMRstructure of YhhP, a novel Escherichia coli protein implicated in cell division
    • Katoh, E., Hatta, T., Shindo, H., Ishii, Y., Yamada, H., Mizuno, T., and Yamazaki, T. (2000) High precisionNMRstructure of YhhP, a novel Escherichia coli protein implicated in cell division. J. Mol. Biol. 304, 219-229
    • (2000) J. Mol. Biol. , vol.304 , pp. 219-229
    • Katoh, E.1    Hatta, T.2    Shindo, H.3    Ishii, Y.4    Yamada, H.5    Mizuno, T.6    Yamazaki, T.7
  • 36
    • 77957342954 scopus 로고    scopus 로고
    • Proteomic analysis of protein-protein interactions within the cysteine sulfinate desulfinase Fe-S cluster biogenesis system
    • Bolstad, H. M., Botelho, D. J., and Wood, M. J. (2010) Proteomic analysis of protein-protein interactions within the cysteine sulfinate desulfinase Fe-S cluster biogenesis system. J. Proteome Res. 9, 5358-5369
    • (2010) J. Proteome Res. , vol.9 , pp. 5358-5369
    • Bolstad, H.M.1    Botelho, D.J.2    Wood, M.J.3


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