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Volumn 390, Issue 4, 2009, Pages 737-746

Crystal Structure of Dinitrogenase Reductase-activating Glycohydrolase (DRAG) Reveals Conservation in the ADP-Ribosylhydrolase Fold and Specific Features in the ADP-Ribose-binding Pocket

Author keywords

ADP ribosylation; Azospirillum brasilense; DraG; nitrogenase; post translational modification

Indexed keywords

ADENOSINE DIPHOSPHATE RIBOSE; ADENOSINE DIPHOSPHATE RIBOSYLHYDROLASE; DINITROGENASE REDUCTASE ACTIVATING GLYCOHYDROLASE; HYDROLASE; MAGNESIUM ION; NITROGENASE; UNCLASSIFIED DRUG;

EID: 67649470390     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.05.031     Document Type: Article
Times cited : (17)

References (32)
  • 4
    • 34547607850 scopus 로고    scopus 로고
    • Nicotinamide adenine dinucleotide: beyond a redox coenzyme
    • Lin H. Nicotinamide adenine dinucleotide: beyond a redox coenzyme. Org. Biomol. Chem. 5 (2007) 2541-2554
    • (2007) Org. Biomol. Chem. , vol.5 , pp. 2541-2554
    • Lin, H.1
  • 5
    • 0028981421 scopus 로고
    • The family of bacterial ADP-ribosylating exotoxins
    • Krueger K.M., and Barbieri J.T. The family of bacterial ADP-ribosylating exotoxins. Clin. Microbiol. Rev. 8 (1995) 34-47
    • (1995) Clin. Microbiol. Rev. , vol.8 , pp. 34-47
    • Krueger, K.M.1    Barbieri, J.T.2
  • 6
    • 0027986527 scopus 로고
    • Reversible ADP-ribosylation as a mechanism of enzyme regulation in procaryotes
    • Ludden P.W. Reversible ADP-ribosylation as a mechanism of enzyme regulation in procaryotes. Mol. Cell. Biochem. 138 (1994) 123-129
    • (1994) Mol. Cell. Biochem. , vol.138 , pp. 123-129
    • Ludden, P.W.1
  • 11
    • 36549065101 scopus 로고    scopus 로고
    • Ternary complex formation between AmtB, GlnZ and the nitrogenase regulatory enzyme DraG reveals a novel facet of nitrogen regulation in bacteria
    • Huergo L.F., Merrick M., Pedrosa F.O., Chubatsu L.S., Araujo L.M., and Souza E.M. Ternary complex formation between AmtB, GlnZ and the nitrogenase regulatory enzyme DraG reveals a novel facet of nitrogen regulation in bacteria. Mol. Microbiol. 66 (2007) 1523-1535
    • (2007) Mol. Microbiol. , vol.66 , pp. 1523-1535
    • Huergo, L.F.1    Merrick, M.2    Pedrosa, F.O.3    Chubatsu, L.S.4    Araujo, L.M.5    Souza, E.M.6
  • 12
    • 65449142921 scopus 로고    scopus 로고
    • II proteins and the nitrogenase regulatory enzymes dinitrogenase reductase ADP-ribosyltransferase (DraT) and dinitrogenase reductase-activating glycohydrolase (DraG) in Azospirillum brasilense
    • II proteins and the nitrogenase regulatory enzymes dinitrogenase reductase ADP-ribosyltransferase (DraT) and dinitrogenase reductase-activating glycohydrolase (DraG) in Azospirillum brasilense. J. Biol. Chem. 284 (2009) 6674-6682
    • (2009) J. Biol. Chem. , vol.284 , pp. 6674-6682
    • Huergo, L.F.1    Merrick, M.2    Monteiro, R.A.3    Chubatsu, L.S.4    Steffens, M.B.5    Pedrosa, F.O.6    Souza, E.M.7
  • 13
    • 28044461261 scopus 로고    scopus 로고
    • Diversity and functional plasticity of eukaryotic selenoproteins: identification and characterization of the SelJ family
    • Castellano S., Lobanov A.V., Chapple C., Novoselov S.V., Albrecht M., Hua D., et al. Diversity and functional plasticity of eukaryotic selenoproteins: identification and characterization of the SelJ family. Proc. Natl Acad. Sci. USA 102 (2005) 16188-16193
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 16188-16193
    • Castellano, S.1    Lobanov, A.V.2    Chapple, C.3    Novoselov, S.V.4    Albrecht, M.5    Hua, D.6
  • 16
    • 33644849513 scopus 로고    scopus 로고
    • Identification and characterization of a mammalian 39-kDa poly(ADP-ribose) glycohydrolase
    • Oka S., Kato J., and Moss J. Identification and characterization of a mammalian 39-kDa poly(ADP-ribose) glycohydrolase. J. Biol. Chem. 281 (2006) 705-713
    • (2006) J. Biol. Chem. , vol.281 , pp. 705-713
    • Oka, S.1    Kato, J.2    Moss, J.3
  • 17
    • 17444383204 scopus 로고
    • Purification of the activating enzyme for the Fe-protein of nitrogenase from Azospirillum brasilense
    • Ljungström E., Yates M.G., and Nordlund S. Purification of the activating enzyme for the Fe-protein of nitrogenase from Azospirillum brasilense. Biochim Biophys. Acta 994 (1989) 210-214
    • (1989) Biochim Biophys. Acta , vol.994 , pp. 210-214
    • Ljungström, E.1    Yates, M.G.2    Nordlund, S.3
  • 18
    • 0003364711 scopus 로고
    • Dependence on divalent cations of the activation of inactive Fe-protein of nitrogenase from Rhodospirillum rubrum
    • Nordlund S., and Norén A. Dependence on divalent cations of the activation of inactive Fe-protein of nitrogenase from Rhodospirillum rubrum. Biochim Biophys. Acta 791 (1984) 21-27
    • (1984) Biochim Biophys. Acta , vol.791 , pp. 21-27
    • Nordlund, S.1    Norén, A.2
  • 19
    • 0022838911 scopus 로고
    • N-Glycohydrolysis of adenosine diphosphoribosyl arginine linkages by dinitrogenase reductase activating glycohydrolase (activating enzyme) from Rhodospirillum rubrum
    • Pope M.R., Saari L.L., and Ludden P.W. N-Glycohydrolysis of adenosine diphosphoribosyl arginine linkages by dinitrogenase reductase activating glycohydrolase (activating enzyme) from Rhodospirillum rubrum. J. Biol. Chem. 261 (1986) 10104-10111
    • (1986) J. Biol. Chem. , vol.261 , pp. 10104-10111
    • Pope, M.R.1    Saari, L.L.2    Ludden, P.W.3
  • 20
    • 0021821712 scopus 로고
    • Covalent modification of the iron protein of nitrogenase from Rhodospirillum rubrum by adenosine diphosphoribosylation of a specific arginine residue
    • Pope M.R., Murrell S.A., and Ludden P.W. Covalent modification of the iron protein of nitrogenase from Rhodospirillum rubrum by adenosine diphosphoribosylation of a specific arginine residue. Proc. Natl Acad. Sci. USA 82 (1985) 3173-3177
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , pp. 3173-3177
    • Pope, M.R.1    Murrell, S.A.2    Ludden, P.W.3
  • 22
    • 0034812439 scopus 로고    scopus 로고
    • Effects of specific amino acid substitutions on activities of dinitrogenase reductase-activating glycohydrolase from Rhodospirillum rubrum
    • Antharavally B.S., Poyner R.R., Zhang Y., Roberts G.P., and Ludden P.W. Effects of specific amino acid substitutions on activities of dinitrogenase reductase-activating glycohydrolase from Rhodospirillum rubrum. J. Bacteriol. 183 (2001) 5743-5746
    • (2001) J. Bacteriol. , vol.183 , pp. 5743-5746
    • Antharavally, B.S.1    Poyner, R.R.2    Zhang, Y.3    Roberts, G.P.4    Ludden, P.W.5
  • 23
    • 0442307833 scopus 로고    scopus 로고
    • Characterization of altered regulation variants of dinitrogenase reductase-activating glycohydrolase from Rhodospirillum rubrum
    • Kim K., Zhang Y., and Roberts G.P. Characterization of altered regulation variants of dinitrogenase reductase-activating glycohydrolase from Rhodospirillum rubrum. FEBS Lett. 559 (2004) 84-88
    • (2004) FEBS Lett. , vol.559 , pp. 84-88
    • Kim, K.1    Zhang, Y.2    Roberts, G.P.3
  • 24
    • 0033546332 scopus 로고    scopus 로고
    • Identification of critical, conserved vicinal aspartate residues in mammalian and bacterial ADP-ribosylarginine hydrolases
    • Konczalik P., and Moss J. Identification of critical, conserved vicinal aspartate residues in mammalian and bacterial ADP-ribosylarginine hydrolases. J. Biol. Chem. 274 (1999) 16736-16740
    • (1999) J. Biol. Chem. , vol.274 , pp. 16736-16740
    • Konczalik, P.1    Moss, J.2
  • 25
    • 27944489552 scopus 로고    scopus 로고
    • Reversible membrane association of dinitrogenase reductase activating glycohydrolase in the regulation of nitrogenase activity in Rhodospirillum rubrum; dependence on GlnJ and AmtB1. FEMS Microbiol
    • Wang H., Franke C.C., Nordlund S., and Noren A. Reversible membrane association of dinitrogenase reductase activating glycohydrolase in the regulation of nitrogenase activity in Rhodospirillum rubrum; dependence on GlnJ and AmtB1. FEMS Microbiol. Lett. 253 (2005) 273-279
    • (2005) Lett. , vol.253 , pp. 273-279
    • Wang, H.1    Franke, C.C.2    Nordlund, S.3    Noren, A.4
  • 27
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch W. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Crystallogr. 26 (1993) 795-800
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 28
    • 14244272868 scopus 로고    scopus 로고
    • PHENIX: building new software for automated crystallographic structure determination. Acta Crystallogr
    • Adams P.D., Grosse-Kunstleve R.W., Hung L.W., Ioerger T.R., McCoy A.J., Moriarty N.W., et al. PHENIX: building new software for automated crystallographic structure determination. Acta Crystallogr. D 58 (2002) 1948-1954
    • (2002) D , vol.58 , pp. 1948-1954
    • Adams, P.D.1    Grosse-Kunstleve, R.W.2    Hung, L.W.3    Ioerger, T.R.4    McCoy, A.J.5    Moriarty, N.W.6
  • 29
    • 33846426122 scopus 로고    scopus 로고
    • Solving structures of protein complexes by molecular replacement with Phaser. Acta Crystallogr
    • McCoy A.J. Solving structures of protein complexes by molecular replacement with Phaser. Acta Crystallogr. D 63 (2007) 32-41
    • (2007) D , vol.63 , pp. 32-41
    • McCoy, A.J.1
  • 30
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P., and Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D 60 (2004) 2126-2132
    • (2004) Acta Crystallogr. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 31
    • 0035182073 scopus 로고    scopus 로고
    • Use of TLS parameters to model anisotropic displacements in macromolecular refinement. Acta Crystallogr
    • Winn M.D., Isupov M.N., and Murshudov G.N. Use of TLS parameters to model anisotropic displacements in macromolecular refinement. Acta Crystallogr. D 57 (2001) 122-133
    • (2001) D , vol.57 , pp. 122-133
    • Winn, M.D.1    Isupov, M.N.2    Murshudov, G.N.3
  • 32
    • 0029315603 scopus 로고
    • MAB, a generally applicable molecular force field for structure modelling in medicinal chemistry
    • Gerber P.R., and Muller K. MAB, a generally applicable molecular force field for structure modelling in medicinal chemistry. J. Comput. Aided Mol. Des. 9 (1995) 251-268
    • (1995) J. Comput. Aided Mol. Des. , vol.9 , pp. 251-268
    • Gerber, P.R.1    Muller, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.