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Volumn 338, Issue 4, 2005, Pages 1935-1942

Crystal structure of C-terminal desundecapeptide nitrite reductase from Achromobacter cycloclastes

Author keywords

C terminal truncation; Copper coordination; Crystal structure; Nitrite reductase; Trimer formation

Indexed keywords

COPPER; METHIONINE; NITRITE REDUCTASE;

EID: 27844463614     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2005.09.199     Document Type: Article
Times cited : (4)

References (29)
  • 1
    • 0031456471 scopus 로고    scopus 로고
    • Cell biology and molecular basis of denitrification
    • W.G. Zumft Cell biology and molecular basis of denitrification Microbiol. Mol. Biol. Rev. 61 1997 533 616
    • (1997) Microbiol. Mol. Biol. Rev. , vol.61 , pp. 533-616
    • Zumft, W.G.1
  • 2
    • 17944403239 scopus 로고    scopus 로고
    • Structure-function relationships of copper-containing nitrite reductases
    • S. Suzuki, K. Kataoka, K. Yamaguchi, T. Inoue, and Y. Kai Structure-function relationships of copper-containing nitrite reductases Coord. Chem. Rev. 190-192 1999 245 265
    • (1999) Coord. Chem. Rev. , vol.190-192 , pp. 245-265
    • Suzuki, S.1    Kataoka, K.2    Yamaguchi, K.3    Inoue, T.4    Kai, Y.5
  • 3
    • 0026353602 scopus 로고
    • The 2.3 angstrom X-ray structure of nitrite reductase from Achromobacter cycloclastes
    • J.W. Godden, S. Turley, D.C. Teller, E.T. Adman, M.Y. Liu, W.J. Payne, and J. LeGall The 2.3 angstrom X-ray structure of nitrite reductase from Achromobacter cycloclastes Science 253 1991 438 442
    • (1991) Science , vol.253 , pp. 438-442
    • Godden, J.W.1    Turley, S.2    Teller, D.C.3    Adman, E.T.4    Liu, M.Y.5    Payne, W.J.6    Legall, J.7
  • 5
    • 0028298314 scopus 로고
    • X-ray structure and site-directed mutagenesis of a nitrite reductase from Alcaligenes faecalis S-6: Roles of two copper atoms in nitrite reduction
    • M. Kukimoto, M. Nishiyama, M.E. Murphy, S. Turley, E.T. Adman, S. Horinouchi, and T. Beppu X-ray structure and site-directed mutagenesis of a nitrite reductase from Alcaligenes faecalis S-6: roles of two copper atoms in nitrite reduction Biochemistry 17 1994 5246 5252
    • (1994) Biochemistry , vol.17 , pp. 5246-5252
    • Kukimoto, M.1    Nishiyama, M.2    Murphy, M.E.3    Turley, S.4    Adman, E.T.5    Horinouchi, S.6    Beppu, T.7
  • 6
    • 0032544483 scopus 로고    scopus 로고
    • X-ray structure of a blue-copper nitrite reductase in two crystal forms. the nature of the copper sites, mode of substrate binding and recognition by redox partner
    • F.E. Dodd, J. Van Beeumen, R.R. Eady, and S.S. Hasnain X-ray structure of a blue-copper nitrite reductase in two crystal forms. The nature of the copper sites, mode of substrate binding and recognition by redox partner J. Mol. Biol. 282 1998 369 382
    • (1998) J. Mol. Biol. , vol.282 , pp. 369-382
    • Dodd, F.E.1    Van Beeumen, J.2    Eady, R.R.3    Hasnain, S.S.4
  • 7
    • 0031786665 scopus 로고    scopus 로고
    • Type 1 Cu structure of blue nitrite reductase from Alcaligenes xylosoxidans GIFU 1051 at 2.05 Å resolution: Comparison of blue and green nitrite reductases
    • T. Inoue, M. Gotowda, Deligeer, K. Kataoka, K. Yamaguchi, S. Suzuki, H. Watanabe, M. Gohow, and Y. Kai Type 1 Cu structure of blue nitrite reductase from Alcaligenes xylosoxidans GIFU 1051 at 2.05 Å resolution: comparison of blue and green nitrite reductases J. Biochem. (Tokyo) 124 1998 876 879
    • (1998) J. Biochem. (Tokyo) , vol.124 , pp. 876-879
    • Inoue, T.1    Gotowda, M.2    Deligeer3    Kataoka, K.4    Yamaguchi, K.5    Suzuki, S.6    Watanabe, H.7    Gohow, M.8    Kai, Y.9
  • 8
    • 0036306042 scopus 로고    scopus 로고
    • Crystal structure of the soluble domain of the major anaerobically induced outer membrane protein (AniA) from pathogenic Neisseria: A new class of copper-containing nitrite reductases
    • M.J. Boulanger, and M.E. Murphy Crystal structure of the soluble domain of the major anaerobically induced outer membrane protein (AniA) from pathogenic Neisseria: a new class of copper-containing nitrite reductases J. Mol. Biol. 315 2002 1111 1127
    • (2002) J. Mol. Biol. , vol.315 , pp. 1111-1127
    • Boulanger, M.J.1    Murphy, M.E.2
  • 9
    • 27844519543 scopus 로고    scopus 로고
    • Structures of the oxidized and reduced forms of nitrite reductase from Rhodobacter sphaeroides 2.4.3 at high pH: Changes in the interactions of the type 2 copper
    • F. Jacobson, H. Guo, K. Olesen, M. Ökvist, R. Neutze, and L. Sjölin Structures of the oxidized and reduced forms of nitrite reductase from Rhodobacter sphaeroides 2.4.3 at high pH: changes in the interactions of the type 2 copper Acta Crystallogr. D 61 2005 1190 1198
    • (2005) Acta Crystallogr. D , vol.61 , pp. 1190-1198
    • Jacobson, F.1    Guo, H.2    Olesen, K.3    Ökvist, M.4    Neutze, R.5    Sjölin, L.6
  • 11
    • 0034097583 scopus 로고    scopus 로고
    • Functional analysis of conserved aspartate and histidine residues located around the type 2 copper site of copper-containing nitrite reductase
    • K. Kataoka, H. Furusawa, K. Takagi, K. Yamaguchi, and S. Suzuki Functional analysis of conserved aspartate and histidine residues located around the type 2 copper site of copper-containing nitrite reductase J. Biochem. (Tokyo) 127 2000 345 350
    • (2000) J. Biochem. (Tokyo) , vol.127 , pp. 345-350
    • Kataoka, K.1    Furusawa, H.2    Takagi, K.3    Yamaguchi, K.4    Suzuki, S.5
  • 12
    • 0034604550 scopus 로고    scopus 로고
    • Catalytic roles for two water bridged residues (Asp-98 and His-255) in the active site of copper-containing nitrite reductase
    • M.J. Boulanger, M. Kukimoto, M. Nishiyama, S. Horinouchi, and M.E. Murphy Catalytic roles for two water bridged residues (Asp-98 and His-255) in the active site of copper-containing nitrite reductase J. Biol. Chem. 275 2000 23957 23964
    • (2000) J. Biol. Chem. , vol.275 , pp. 23957-23964
    • Boulanger, M.J.1    Kukimoto, M.2    Nishiyama, M.3    Horinouchi, S.4    Murphy, M.E.5
  • 13
    • 0035822630 scopus 로고    scopus 로고
    • Alternate substrate binding modes to two mutant (D98N and H255N) forms of nitrite reductase from Alcaligenes faecalis S-6: Structural model of a transient catalytic intermediate
    • M.J. Boulanger, and M.E. Murphy Alternate substrate binding modes to two mutant (D98N and H255N) forms of nitrite reductase from Alcaligenes faecalis S-6: structural model of a transient catalytic intermediate Biochemistry 40 2001 9132 9141
    • (2001) Biochemistry , vol.40 , pp. 9132-9141
    • Boulanger, M.J.1    Murphy, M.E.2
  • 14
    • 0027223884 scopus 로고
    • X-ray scattering using synchrotron radiation shows nitrite reductase from Achromobacter xylosoxidans to be a trimer in solution
    • J.G. Grossmann, Z.H. Abraham, E.T. Adman, M. Neu, R.R. Eady, B.E. Smith, and S.S. Hasnain X-ray scattering using synchrotron radiation shows nitrite reductase from Achromobacter xylosoxidans to be a trimer in solution Biochemistry 32 1993 7360 7366
    • (1993) Biochemistry , vol.32 , pp. 7360-7366
    • Grossmann, J.G.1    Abraham, Z.H.2    Adman, E.T.3    Neu, M.4    Eady, R.R.5    Smith, B.E.6    Hasnain, S.S.7
  • 15
    • 0032578587 scopus 로고    scopus 로고
    • The C-terminal segment is essential for maintaining the quaternary structure and enzyme activity of the nitric oxide forming nitrite reductase from Achromobacter cycloclastes
    • W.C. Chang, J.Y. Chen, T. Chang, M.Y. Liu, W.J. Payne, J. LeGall, and W.C. Chang The C-terminal segment is essential for maintaining the quaternary structure and enzyme activity of the nitric oxide forming nitrite reductase from Achromobacter cycloclastes Biochem. Biophys. Res. Commun. 250 1998 782 785
    • (1998) Biochem. Biophys. Res. Commun. , vol.250 , pp. 782-785
    • Chang, W.C.1    Chen, J.Y.2    Chang, T.3    Liu, M.Y.4    Payne, W.J.5    Legall, J.6    Chang, W.C.7
  • 16
    • 0019457194 scopus 로고
    • Purification and properties of a copper-containing nitrite reductase from a denitrifying bacterium, Alcaligenes faecalis strain S-6
    • T. Kakutani, H. Watanabe, K. Arima, and T. Beppu Purification and properties of a copper-containing nitrite reductase from a denitrifying bacterium, Alcaligenes faecalis strain S-6 J. Biochem. 89 1981 453 461
    • (1981) J. Biochem. , vol.89 , pp. 453-461
    • Kakutani, T.1    Watanabe, H.2    Arima, K.3    Beppu, T.4
  • 18
    • 0036435122 scopus 로고    scopus 로고
    • Preliminary crystallographic studies of two C-terminally truncated copper-containing nitrite reductases from Achromobacter cycloclastes: Changed crystallizing behaviors caused by residue deletion
    • H.T. Li, T. Chang, M.Y. Liu, J. LeGall, X.M. An, L.L. Gui, J.P. Zhang, D.C. Liang, and W.R. Chang Preliminary crystallographic studies of two C-terminally truncated copper-containing nitrite reductases from Achromobacter cycloclastes: changed crystallizing behaviors caused by residue deletion Biochem. Biophys. Res. Commun. 299 2002 173 176
    • (2002) Biochem. Biophys. Res. Commun. , vol.299 , pp. 173-176
    • Li, H.T.1    Chang, T.2    Liu, M.Y.3    Legall, J.4    An, X.M.5    Gui, L.L.6    Zhang, J.P.7    Liang, D.C.8    Chang, W.R.9
  • 19
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Z. Otwinowski, and W. Minor Processing of X-ray diffraction data collected in oscillation mode Methods Enzymol. 276 1996 307 326
    • (1996) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 20
    • 84920325457 scopus 로고
    • Amore: An automated package for molecular replacement
    • J. Navaza Amore: an automated package for molecular replacement Acta Crystallogr. A 50 1994 157 163
    • (1994) Acta Crystallogr. a , vol.50 , pp. 157-163
    • Navaza, J.1
  • 22
    • 0029644940 scopus 로고
    • Where freedom is given, liberties are taken
    • G.J. Kleywegt, and T.A. Jones Where freedom is given, liberties are taken Structure 3 1995 535 540
    • (1995) Structure , vol.3 , pp. 535-540
    • Kleywegt, G.J.1    Jones, T.A.2
  • 23
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • T.A. Jones, J.Y. Zou, S.W. Cowan, and Kjeldgaard Improved methods for building protein models in electron density maps and the location of errors in these models Acta Crystallogr. A 47 1991 110 119
    • (1991) Acta Crystallogr. a , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard4
  • 25
    • 0026701748 scopus 로고
    • Evidence that the type 2 copper centers are the site of nitrite reduction by Achromobacter cycloclastes nitrite reductase
    • E. Libby, and B.A. Averill Evidence that the type 2 copper centers are the site of nitrite reduction by Achromobacter cycloclastes nitrite reductase Biochem. Biophys. Res. Commun. 187 1992 1529 1535
    • (1992) Biochem. Biophys. Res. Commun. , vol.187 , pp. 1529-1535
    • Libby, E.1    Averill, B.A.2
  • 26
    • 8444245920 scopus 로고    scopus 로고
    • Characterization of two type 1 Cu sites of Hyphomicrobium denitrificans nitrite reductase: A new class of copper-containing nitrite reductases
    • K. Yamaguchi, K. Kataoka, M. Kobayashi, K. Itoh, A. Fukui, and S. Suzuki Characterization of two type 1 Cu sites of Hyphomicrobium denitrificans nitrite reductase: a new class of copper-containing nitrite reductases Biochemistry 43 2004 14180 14188
    • (2004) Biochemistry , vol.43 , pp. 14180-14188
    • Yamaguchi, K.1    Kataoka, K.2    Kobayashi, M.3    Itoh, K.4    Fukui, A.5    Suzuki, S.6
  • 27
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • P.J. Kraulis MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures J. Appl. Crystallogr. 24 1991 946 950
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 28
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • E.A Merritt, and D.J. Bacon Raster3D: photorealistic molecular graphics Methods Enzymol. 277 1997 505 524
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 29
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • N. Guex, and M.C. Peitsch SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling Electrophoresis 18 1997 2714 2723
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2


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