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Volumn 325, Issue 3, 2003, Pages 471-483

Crystal structure and site-directed mutagenesis of enzymatic components from Clostridium perfringens Iota-toxin

Author keywords

Actin; ADP ribosyltransferase; Iota toxin; NMN ring like conformation; Sn1 type reaction

Indexed keywords

AMINO ACID; ARGININE; ASPARAGINE; BACTERIAL TOXIN; GLUTAMIC ACID; IOTA TOXIN; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; NICOTINAMIDE ADENINE DINUCLEOTIDE NUCLEOSIDASE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; PHENYLALANINE; PROTEIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; SERINE; TYROSINE; UNCLASSIFIED DRUG; VEGETATIVE INSECTIDAL PROTEIN;

EID: 0037225397     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(02)01247-0     Document Type: Article
Times cited : (91)

References (41)
  • 1
    • 0012425066 scopus 로고
    • Observation on association between Clostridium spiroforme and Clostridium perfringens type E iota enterotoxaemia in rabbits
    • Carman, R. J. & Borriello, S. P. (1982). Observation on association between Clostridium spiroforme and Clostridium perfringens type E iota enterotoxaemia in rabbits. Eur. J. Chemother. Antibiol. 2, 143-144.
    • (1982) Eur. J. Chemother. Antibiol. , vol.2 , pp. 143-144
    • Carman, R.J.1    Borriello, S.P.2
  • 2
    • 0019180204 scopus 로고
    • Enterotoxaemia involving Clostridium perfringens iota toxin in a hysterectomy-derived rabbit colony
    • Eaton, P. & Fernie, D. S. (1980). Enterotoxaemia involving Clostridium perfringens iota toxin in a hysterectomy-derived rabbit colony. Lab. Anim. 14, 347-351.
    • (1980) Lab. Anim. , vol.14 , pp. 347-351
    • Eaton, P.1    Fernie, D.S.2
  • 3
    • 0020658445 scopus 로고
    • Association of iota-like toxin and Clostridium spiroforme with both spontaneous and antibiotic-associated diarrhea and colitis in rabbits
    • Borriello, S. P. & Carman, R. J. (1983). Association of iota-like toxin and Clostridium spiroforme with both spontaneous and antibiotic-associated diarrhea and colitis in rabbits. J. Clin. Microbiol. 17, 414-418.
    • (1983) J. Clin. Microbiol. , vol.17 , pp. 414-418
    • Borriello, S.P.1    Carman, R.J.2
  • 4
    • 0028804183 scopus 로고
    • Toxins of Clostridium perfringens
    • Sakurai, J. (1995). Toxins of Clostridium perfringens. Rev. Ned. Microbiol. 6, 175-185.
    • (1995) Rev. Ned. Microbiol. , vol.6 , pp. 175-185
    • Sakurai, J.1
  • 5
    • 0028952871 scopus 로고
    • Lethal and dermonecrotic activities of Clostridium perfringens iota toxin: Biological activities induced by cooperation of two nonlinked components
    • Sakurai, J. & Kobayashi, K. (1995). Lethal and dermonecrotic activities of Clostridium perfringens iota toxin: Biological activities induced by cooperation of two nonlinked components. Microbiol. Immunol. 39, 249-253.
    • (1995) Microbiol. Immunol. , vol.39 , pp. 249-253
    • Sakurai, J.1    Kobayashi, K.2
  • 6
    • 0001993075 scopus 로고
    • Mechanism of action of cholera toxin
    • Moss, J. & Vaughan, M., eds, American Society for Microbiology, Washington DC
    • Fishman, P. H. (1990). Mechanism of action of cholera toxin. In ADP-ribosylating Toxins and G Proteins (Moss, J. & Vaughan, M., eds), pp. 127-140, American Society for Microbiology, Washington DC.
    • (1990) ADP-ribosylating Toxins and G Proteins , pp. 127-140
    • Fishman, P.H.1
  • 7
    • 0026609066 scopus 로고
    • Diphtheria toxin and Pseudomonas aeruginosa exotoxin A: Active-site structure and enzymic mechanism
    • Wilson, B. A. & Collier, R. J. (1992). Diphtheria toxin and Pseudomonas aeruginosa exotoxin A: Active-site structure and enzymic mechanism. Curr. Top. Microbiol. Immunol. 175, 27-41.
    • (1992) Curr. Top. Microbiol. Immunol. , vol.175 , pp. 27-41
    • Wilson, B.A.1    Collier, R.J.2
  • 8
    • 0023882163 scopus 로고
    • Botulinum ADP-ribosyltransferase C3. Purification of the enzyme and characterization of the ADP-ribosylation reaction in platelet membranes
    • Aktories, K., Rosener, S., Blaschke, U. & Chhatwal, G. S. (1988). Botulinum ADP-ribosyltransferase C3. Purification of the enzyme and characterization of the ADP-ribosylation reaction in platelet membranes. Eur. J. Biochem. 172, 445-450.
    • (1988) Eur. J. Biochem. , vol.172 , pp. 445-450
    • Aktories, K.1    Rosener, S.2    Blaschke, U.3    Chhatwal, G.S.4
  • 10
    • 0023024730 scopus 로고
    • Purification and characterization of Clostridium perfringens iota toxin: Dependence on two nonlinked proteins for biological activity
    • Stiles, B. G. & Wilkins, T. D. (1986). Purification and characterization of Clostridium perfringens iota toxin: Dependence on two nonlinked proteins for biological activity. Infect. Immun. 54, 683-688.
    • (1986) Infect. Immun. , vol.54 , pp. 683-688
    • Stiles, B.G.1    Wilkins, T.D.2
  • 11
    • 0023942902 scopus 로고
    • Clostridium spiroforme toxin is a binary toxin which ADP-ribosylates cellular actin
    • Popoff, M. R. & Boquet, P. (1988). Clostridium spiroforme toxin is a binary toxin which ADP-ribo-sylates cellular actin. Biochem. Biophys. Res. Commun. 152, 1361-1368.
    • (1988) Biochem. Biophys. Res. Commun. , vol.152 , pp. 1361-1368
    • Popoff, M.R.1    Boquet, P.2
  • 12
    • 0023747353 scopus 로고
    • Actin-specific ADP-ribosyltransferase produced by a Clostridium difficile strain
    • Popoff, M. R., Rubin, E. J., Gill, D. M. & Boquet, P. (1988). Actin-specific ADP-ribosyltransferase produced by a Clostridium difficile strain. Infect. Immun. 56 , 2299-2306.
    • (1988) Infect. Immun. , vol.56 , pp. 2299-2306
    • Popoff, M.R.1    Rubin, E.J.2    Gill, D.M.3    Boquet, P.4
  • 13
    • 0023830603 scopus 로고
    • ADP-ribosylation of skeletal muscle and non-muscle actin by Clostridium perfringens iota toxin
    • Schering, B., Barmann, M., Chhatwal, G. S., Geipel, U. & Aktories, K. (1988). ADP-ribosylation of skeletal muscle and non-muscle actin by Clostridium perfringens iota toxin. Eur. J. Biochem. 171, 225-229.
    • (1988) Eur. J. Biochem. , vol.171 , pp. 225-229
    • Schering, B.1    Barmann, M.2    Chhatwal, G.S.3    Geipel, U.4    Aktories, K.5
  • 14
    • 0025242426 scopus 로고
    • ADP-ribosylation of actin isoforms by Clostridium botulinum C2 toxin and Clostridium perfringens iota toxin
    • Mauss, S., Chaponnier, C., Just, I., Aktories, K. & Gabbiani, G. (1990). ADP-ribosylation of actin isoforms by Clostridium botulinum C2 toxin and Clostridium perfringens iota toxin. Eur. J. Biochem. 194, 237-241.
    • (1990) Eur. J. Biochem. , vol.194 , pp. 237-241
    • Mauss, S.1    Chaponnier, C.2    Just, I.3    Aktories, K.4    Gabbiani, G.5
  • 15
    • 0034029903 scopus 로고    scopus 로고
    • Characterization of the enzymatic component of Clostridium perfringens iota-toxin
    • Nagahama, M., Sakaguchi, Y., Kobayashi, K., Ochi, S. & Sakurai, J. (2000). Characterization of the enzymatic component of Clostridium perfringens iota-toxin. J. Bacteriol. 182, 2096-2103.
    • (2000) J. Bacteriol. , vol.182 , pp. 2096-2103
    • Nagahama, M.1    Sakaguchi, Y.2    Kobayashi, K.3    Ochi, S.4    Sakurai, J.5
  • 16
    • 0032491480 scopus 로고    scopus 로고
    • Characterization of the catalytic site of the ADP-ribosyltransferase Clostridium botulinum C2 toxin by site-directed mutagenesis
    • Barth, H., Preiss, J. C., Hofmann, F. & Aktories, K. (1998). Characterization of the catalytic site of the ADP-ribosyltransferase Clostridium botulinum C2 toxin by site-directed mutagenesis. J. Biol. Chem. 273, 29506-29511.
    • (1998) J. Biol. Chem. , vol.273 , pp. 29506-29511
    • Barth, H.1    Preiss, J.C.2    Hofmann, F.3    Aktories, K.4
  • 17
    • 0032876380 scopus 로고    scopus 로고
    • Evolution and mechanism from structures of an ADP-ribosylating toxin and NAD complex
    • Han, S., Craig, J. A., Putnam, C. D., Carozzi, N. B. & Tainer, J. A. (1999). Evolution and mechanism from structures of an ADP-ribosylating toxin and NAD complex. Nature Struct. Biol. 6, 932-936.
    • (1999) Nature Struct. Biol. , vol.6 , pp. 932-936
    • Han, S.1    Craig, J.A.2    Putnam, C.D.3    Carozzi, N.B.4    Tainer, J.A.5
  • 18
    • 0028103275 scopus 로고
    • The CCP4 suite
    • Collaborative Computational Project Number 4 (1994). The CCP4 suite. Acta Crysatallog. Sect. D, 50, 760-763.
    • (1994) Acta Crysatallog. Sect. D , vol.50 , pp. 760-763
  • 19
    • 0037163040 scopus 로고    scopus 로고
    • NAD binding induces conformational changes in Rho ADP-ribosylating clostridium botulinum C3 exoenzyme
    • Menetrey, J., Flatau, G., Stura, E. A., Charbonnier, J. B., Gas, F., Teulon, J. M. et al. (2002). NAD binding induces conformational changes in Rho ADP-ribo-sylating clostridium botulinum C3 exoenzyme. J. Biol. Chem. 277, 30950-30957.
    • (2002) J. Biol. Chem. , vol.277 , pp. 30950-30957
    • Menetrey, J.1    Flatau, G.2    Stura, E.A.3    Charbonnier, J.B.4    Gas, F.5    Teulon, J.M.6
  • 20
    • 0035808303 scopus 로고    scopus 로고
    • Crystal structure and novel recognition motif of rho ADP-ribosylating C3 exoenzyme from Clostridium botulinum: Structural insights for recognition specificity and catalysis
    • Han, S., Arvai, A. S., Clancy, S. B. & Tainer, J. A. (2001). Crystal structure and novel recognition motif of rho ADP-ribosylating C3 exoenzyme from Clostridium botulinum: Structural insights for recognition specificity and catalysis. J. Mol. Biol. 305, 95-107.
    • (2001) J. Mol. Biol. , vol.305 , pp. 95-107
    • Han, S.1    Arvai, A.S.2    Clancy, S.B.3    Tainer, J.A.4
  • 22
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm, L. & Sander, C. (1993). Protein structure comparison by alignment of distance matrices. J. Mol. Biol. 233, 123-138.
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 23
    • 0031037322 scopus 로고    scopus 로고
    • Crystal structure of nucleotide-free diphtheria toxin
    • Bell, C. E. & Eisenberg, D. (1997). Crystal structure of nucleotide-free diphtheria toxin. Biochemistry, 36, 481-488.
    • (1997) Biochemistry , vol.36 , pp. 481-488
    • Bell, C.E.1    Eisenberg, D.2
  • 24
    • 0027945840 scopus 로고
    • Common structure of catalytic sites of mammalian and bacterial toxin ADP-ribosyltransferases
    • Okazaki, I. J. & Moss, J. (1994). Common structure of catalytic sites of mammalian and bacterial toxin ADP-ribosyltransferases. Mol. Cell. Biochem. 138, 177-181.
    • (1994) Mol. Cell. Biochem. , vol.138 , pp. 177-181
    • Okazaki, I.J.1    Moss, J.2
  • 25
    • 0029746051 scopus 로고    scopus 로고
    • Three conserved consensus sequences identify the NAD-binding site of ADP-ribosylating enzymes, expressed by eukaryotes, bacteria and T-even bacteriophages
    • Domenighini, M. & Rappuoli, R. (1996). Three conserved consensus sequences identify the NAD-binding site of ADP-ribosylating enzymes, expressed by eukaryotes, bacteria and T-even bacteriophages. Mol. Microbiol. 21, 667-674.
    • (1996) Mol. Microbiol. , vol.21 , pp. 667-674
    • Domenighini, M.1    Rappuoli, R.2
  • 26
    • 0025076421 scopus 로고
    • Active-site mutations of diphtheria toxin: Effects of replacing glutamic acid-148 with aspartic acid, glutamine, or serine
    • Wilson, B. A., Reich, K. A., Weinstein, B. R. & Collier, R. J. (1990). Active-site mutations of diphtheria toxin: Effects of replacing glutamic acid-148 with aspartic acid, glutamine, or serine. Biochemistry, 29, 8643-8651.
    • (1990) Biochemistry , vol.29 , pp. 8643-8651
    • Wilson, B.A.1    Reich, K.A.2    Weinstein, B.R.3    Collier, R.J.4
  • 27
    • 0002325285 scopus 로고
    • Synthesis of glycosides
    • Trost, B. M. & Fleming, I., eds, Pergamon Press, New York
    • Schmidt, R. (1991). Synthesis of glycosides. In Comprehensive Organic Synthesis (Trost, B. M. & Fleming, I., eds), vol. 6, pp. 33-61, Pergamon Press, New York.
    • (1991) Comprehensive Organic Synthesis , vol.6 , pp. 33-61
    • Schmidt, R.1
  • 28
    • 0030050341 scopus 로고    scopus 로고
    • Analysis of the catalytic site of the actin ADP-ribosylating Clostridium perfringens iota toxin
    • van Damme, J., Jung, M., Hofmann, F., Just, I., Vandekerckhove, J. & Aktories, K. (1996). Analysis of the catalytic site of the actin ADP-ribosylating Clostridium perfringens iota toxin. FEBS Letters, 380, 291-295.
    • (1996) FEBS Letters , vol.380 , pp. 291-295
    • Van Damme, J.1    Jung, M.2    Hofmann, F.3    Just, I.4    Vandekerckhove, J.5    Aktories, K.6
  • 29
    • 0028916854 scopus 로고
    • Site-directed muta-genesis of histidine residues in Clostridium perfringens alpha-toxin
    • Nagahama, M., Okagawa, Y., Nakayama, T., Nishioka, E. & Sakurai, J. (1995). Site-directed muta-genesis of histidine residues in Clostridium perfringens alpha-toxin. J. Bacteriol. 177, 1179-1185.
    • (1995) J. Bacteriol. , vol.177 , pp. 1179-1185
    • Nagahama, M.1    Okagawa, Y.2    Nakayama, T.3    Nishioka, E.4    Sakurai, J.5
  • 30
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. & 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
  • 31
    • 0002414103 scopus 로고
    • Molecular data processing
    • Moras, D., Podjarny, A. D. & Thierry, J. C., eds, Oxford University Press, New York
    • Leslie, A. G. W. (1990). Molecular data processing. In Crystallographic Computing (Moras, D., Podjarny, A. D. & Thierry, J. C., eds), vol. 5, Oxford University Press, New York.
    • (1990) Crystallographic Computing , vol.5
    • Leslie, A.G.W.1
  • 33
    • 84889120137 scopus 로고
    • Improved methods for binding protein models in electron density maps and the location of errors in these models
    • Jones, T. A., Zou, J. Y., Cowan, S. W. & Kjeldgaard, M. (1991). Improved methods for binding protein models in electron density maps and the location of errors in these models. Acta Crystallog. Sect. A, 47, 110-119.
    • (1991) Acta Crystallog. Sect. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 35
    • 0026597444 scopus 로고
    • Free R value: A novel statistical quantity for assessing the accuracy of the crystal structures
    • Brunger, A. T. (1992). Free R value: A novel statistical quantity for assessing the accuracy of the crystal structures. Nature, 335, 472-474.
    • (1992) Nature , vol.335 , pp. 472-474
    • Brunger, A.T.1
  • 36
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structure
    • Laskowski, R. A., MacArthur, M. W., Moss, D. S. & Thornton, J. M. (1993). PROCHECK: A program to check the stereochemical quality of protein structure. J. Appl. Crystallog. 26, 283-291.
    • (1993) J. Appl. Crystallog. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 37
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. (1991). MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24, 946-950.
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.1
  • 38
    • 0028057108 scopus 로고
    • RASTER3D version2.0, a program for photorealistic molecular graphics
    • Merritt, E. A. & Murphy, M. E. P. (1994). RASTER3D version2.0, a program for photorealistic molecular graphics. Acta Crysatallog. Sect. D, 50, 869-873.
    • (1994) Acta Crysatallog. Sect. D , vol.50 , pp. 869-873
    • Merritt, E.A.1    Murphy, M.E.P.2
  • 39
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit - A versatile program for manipulating atomic coordinates and electron density
    • McRee, D. E. (1999). XtalView/Xfit - A versatile program for manipulating atomic coordinates and electron density. J. Struct. Biol. 125, 156-165.
    • (1999) J. Struct. Biol. , vol.125 , pp. 156-165
    • McRee, D.E.1
  • 40
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K. A. & Honig, B. (1991). Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins, 11, 281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 41
    • 0028922586 scopus 로고
    • LIGPLOT: A program to generate schematic diagrams of protein-ligand interactions
    • Wallace, A. C., Laskowski, R. A. & Thornton, J. M. (1995). LIGPLOT: A program to generate schematic diagrams of protein-ligand interactions. Protein. Eng. 8, 127-134.
    • (1995) Protein. Eng. , vol.8 , pp. 127-134
    • Wallace, A.C.1    Laskowski, R.A.2    Thornton, J.M.3


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