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Volumn 288, Issue 33, 2013, Pages 24223-24233

The C terminus of the catalytic domain of type A botulinum neurotoxin may facilitate product release from the active site

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; BIOLOGY;

EID: 84882431363     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.451286     Document Type: Article
Times cited : (21)

References (48)
  • 3
    • 0037193993 scopus 로고    scopus 로고
    • Aromatic residues in the C-terminal region of glutathione transferase A1-1 influence rate-determining steps in the catalytic mechanism
    • Nilsson, L. O., Edalat, M., Pettersson, P. L., and Mannervik, B. (2002) Aromatic residues in the C-terminal region of glutathione transferase A1-1 influence rate-determining steps in the catalytic mechanism. Biochim. Biophys. Acta 1598, 199-205
    • (2002) Biochim. Biophys. Acta , vol.1598 , pp. 199-205
    • Nilsson, L.O.1    Edalat, M.2    Pettersson, P.L.3    Mannervik, B.4
  • 4
    • 77954588113 scopus 로고    scopus 로고
    • 1H NMR study of the influence of mutation on the interaction of the C-terminus with the active site in heme oxygenase from Neisseria meningitidis: Implications for product release
    • Peng, D., Ma, L. H., Ogura, H., Yang, E. C., Zhang, X., Yoshida, T., and La Mar, G. N. (2010) 1H NMR study of the influence of mutation on the interaction of the C-terminus with the active site in heme oxygenase from Neisseria meningitidis: implications for product release. Biochemistry 49, 5832-5840
    • (2010) Biochemistry , vol.49 , pp. 5832-5840
    • Peng, D.1    Ma, L.H.2    Ogura, H.3    Yang, E.C.4    Zhang, X.5    Yoshida, T.6    La Mar, G.N.7
  • 6
    • 79952182929 scopus 로고    scopus 로고
    • An intrinsically disordered C terminus allows the la protein to assist the biogenesis of diverse noncoding RNA precursors
    • Kucera, N. J., Hodsdon, M. E., and Wolin, S. L. (2011) An intrinsically disordered C terminus allows the La protein to assist the biogenesis of diverse noncoding RNA precursors. Proc. Natl. Acad. Sci. U.S.A. 108, 1308-1313
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 1308-1313
    • Kucera, N.J.1    Hodsdon, M.E.2    Wolin, S.L.3
  • 7
    • 84859386736 scopus 로고    scopus 로고
    • Intrinsically disordered N-terminus of calponin homology-associated smooth muscle protein (CHASM) interacts with the calponin homology domain to enable tropomyosin binding
    • MacDonald, J. A., Ishida, H., Butler, E. I., Ulke-Lemée, A., Chappellaz, M., Tulk, S. E., Chik, J. K., and Vogel, H. J. (2012) Intrinsically disordered N-terminus of calponin homology-associated smooth muscle protein (CHASM) interacts with the calponin homology domain to enable tropomyosin binding. Biochemistry 51, 2694-2705
    • (2012) Biochemistry , vol.51 , pp. 2694-2705
    • Macdonald, J.A.1    Ishida, H.2    Butler, E.I.3    Ulke-Lemée, A.4    Chappellaz, M.5    Tulk, S.E.6    Chik, J.K.7    Vogel, H.J.8
  • 8
    • 77958482255 scopus 로고    scopus 로고
    • The N-terminus of the intrinsically disordered protein-synuclein triggers membrane binding and helix folding
    • Bartels, T., Ahlstrom, L. S., Leftin, A., Kamp, F., Haass, C., Brown, M. F., and Beyer, K. (2010) The N-terminus of the intrinsically disordered protein-synuclein triggers membrane binding and helix folding. Biophys. J. 99, 2116-2124
    • (2010) Biophys. J. , vol.99 , pp. 2116-2124
    • Bartels, T.1    Ahlstrom, L.S.2    Leftin, A.3    Kamp, F.4    Haass, C.5    Brown, M.F.6    Beyer, K.7
  • 9
    • 0031712779 scopus 로고    scopus 로고
    • Crystal structure of botulinum neurotoxin type A and implications for toxicity
    • Lacy, D. B., Tepp, W., Cohen, A. C., DasGupta, B. R., and Stevens, R. C. (1998) Crystal structure of botulinum neurotoxin type A and implications for toxicity. Nat. Struct. Biol. 5, 898-902
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 898-902
    • Lacy, D.B.1    Tepp, W.2    Cohen, A.C.3    Dasgupta, B.R.4    Stevens, R.C.5
  • 10
    • 0025167248 scopus 로고
    • Botulinum neurotoxin type A: Sequence of amino acids at the N-terminus and around the nicking site
    • DasGupta, B. R., and Dekleva, M. L. (1990) Botulinum neurotoxin type A: sequence of amino acids at the N-terminus and around the nicking site. Biochimie 72, 661-664
    • (1990) Biochimie , vol.72 , pp. 661-664
    • Dasgupta, B.R.1    Dekleva, M.L.2
  • 11
    • 0028204552 scopus 로고
    • Covalent structure of botulinum neurotoxin type A: Location of sulfhydryl groups, and disulfide bridges and identification of C-termini of light and heavy chains
    • Krieglstein, K. G., DasGupta, B. R., and Henschen, A. H. (1994) Covalent structure of botulinum neurotoxin type A: location of sulfhydryl groups, and disulfide bridges and identification of C-termini of light and heavy chains. J. Protein Chem. 13, 49-57
    • (1994) J. Protein Chem. , vol.13 , pp. 49-57
    • Krieglstein, K.G.1    Dasgupta, B.R.2    Henschen, A.H.3
  • 12
    • 49649121294 scopus 로고    scopus 로고
    • Structure-and substrate-based inhibitor design for Clostridium botulinum neurotoxin serotype A
    • Kumaran, D., Rawat, R., Ludivico, M. L., Ahmed, S. A., and Swaminathan, S. (2008) Structure-and substrate-based inhibitor design for Clostridium botulinum neurotoxin serotype A. J. Biol. Chem. 283, 18883-18891
    • (2008) J. Biol. Chem. , vol.283 , pp. 18883-18891
    • Kumaran, D.1    Rawat, R.2    Ludivico, M.L.3    Ahmed, S.A.4    Swaminathan, S.5
  • 13
    • 44349178037 scopus 로고    scopus 로고
    • Catalytic features of the botulinum neurotoxin A light chain revealed by high resolution structure of an inhibitory peptide complex
    • Silvaggi, N. R., Wilson, D., Tzipori, S., and Allen, K. N. (2008) Catalytic features of the botulinum neurotoxin A light chain revealed by high resolution structure of an inhibitory peptide complex. Biochemistry 47, 5736-5745
    • (2008) Biochemistry , vol.47 , pp. 5736-5745
    • Silvaggi, N.R.1    Wilson, D.2    Tzipori, S.3    Allen, K.N.4
  • 14
    • 84867568308 scopus 로고    scopus 로고
    • Inhibition of catalytic activities of botulinum neurotoxin light chains of serotypes A, B and e by acetate, sulfate and calcium
    • Mizanur, R. M., Gorbet, J., Swaminathan, S., and Ahmed, S. A. (2012) Inhibition of catalytic activities of botulinum neurotoxin light chains of serotypes A, B and E by acetate, sulfate and calcium. IJBMB 3, 313-321
    • (2012) IJBMB , vol.3 , pp. 313-321
    • Mizanur, R.M.1    Gorbet, J.2    Swaminathan, S.3    Ahmed, S.A.4
  • 15
    • 11144341950 scopus 로고    scopus 로고
    • Substrate recognition strategy for botulinum neurotoxin serotype A
    • Breidenbach, M. A., and Brunger, A. T. (2004) Substrate recognition strategy for botulinum neurotoxin serotype A. Nature 432, 925-929
    • (2004) Nature , vol.432 , pp. 925-929
    • Breidenbach, M.A.1    Brunger, A.T.2
  • 16
    • 43249094415 scopus 로고    scopus 로고
    • Identification of residues surrounding the active site of type A botulinum neurotoxin important for substrate recognition and catalytic activity
    • Ahmed, S. A., Olson, M. A., Ludivico, M. L., Gilsdorf, J., and Smith, L. A. (2008) Identification of residues surrounding the active site of type A botulinum neurotoxin important for substrate recognition and catalytic activity. Protein J. 27, 151-162
    • (2008) Protein J. , vol.27 , pp. 151-162
    • Ahmed, S.A.1    Olson, M.A.2    Ludivico, M.L.3    Gilsdorf, J.4    Smith, L.A.5
  • 17
    • 53049093960 scopus 로고    scopus 로고
    • Substrate binding mode and its implication on drug design for botulinum neurotoxin A
    • Kumaran, D., Rawat, R., Ahmed, S. A., and Swaminathan, S. (2008) Substrate binding mode and its implication on drug design for botulinum neurotoxin A. PLoS Pathog. 4, e1000165
    • (2008) PLoS Pathog. , vol.4
    • Kumaran, D.1    Rawat, R.2    Ahmed, S.A.3    Swaminathan, S.4
  • 18
    • 3543058813 scopus 로고    scopus 로고
    • The C-terminus of botulinum neurotoxin type A light chain contributes to solubility, catalysis, and stability
    • Baldwin, M. R., Bradshaw, M., Johnson, E. A., and Barbieri, J. T. (2004) The C-terminus of botulinum neurotoxin type A light chain contributes to solubility, catalysis, and stability. Protein Expr. Purif. 37, 187-195
    • (2004) Protein Expr. Purif. , vol.37 , pp. 187-195
    • Baldwin, M.R.1    Bradshaw, M.2    Johnson, E.A.3    Barbieri, J.T.4
  • 21
    • 69949102167 scopus 로고    scopus 로고
    • Pharmacophoreguided lead optimization: The rational design of a non-zinc coordinating, sub-micromolar inhibitor of the botulinum neurotoxin serotype a metalloprotease
    • Burnett, J. C., Wang, C., Nuss, J. E., Nguyen, T. L., Hermone, A. R., Schmidt, J. J., Gussio, R., Wipf, P., and Bavari, S. (2009) Pharmacophoreguided lead optimization: the rational design of a non-zinc coordinating, sub-micromolar inhibitor of the botulinum neurotoxin serotype a metalloprotease. Bioorg. Med. Chem. Lett. 19, 5811-5813
    • (2009) Bioorg. Med. Chem. Lett. , vol.19 , pp. 5811-5813
    • Burnett, J.C.1    Wang, C.2    Nuss, J.E.3    Nguyen, T.L.4    Hermone, A.R.5    Schmidt, J.J.6    Gussio, R.7    Wipf, P.8    Bavari, S.9
  • 24
    • 28444438140 scopus 로고    scopus 로고
    • Botulinum neurotoxin types A, B, and E: Fragmentations by autoproteolysis and other mechanisms including by O-phenanthroline-dithiothreitol, and association of the dinucleotides NAD/NADH with the heavy chain of the three neurotoxins
    • Dasgupta, B. R., Antharavally, B. S., Tepp, W., and Evenson, M. L. (2005) Botulinum neurotoxin types A, B, and E: fragmentations by autoproteolysis and other mechanisms including by O-phenanthroline-dithiothreitol, and association of the dinucleotides NAD/NADH with the heavy chain of the three neurotoxins. Protein J. 24, 337-368
    • (2005) Protein J. , vol.24 , pp. 337-368
    • Dasgupta, B.R.1    Antharavally, B.S.2    Tepp, W.3    Evenson, M.L.4
  • 25
    • 0242381350 scopus 로고    scopus 로고
    • Autocatalytically fragmented light chain of botulinum A neurotoxin is enzymatically active
    • Ahmed, S. A., McPhie, P., and Smith, L. A. (2003) Autocatalytically fragmented light chain of botulinum A neurotoxin is enzymatically active. Biochemistry 42, 12539-12549
    • (2003) Biochemistry , vol.42 , pp. 12539-12549
    • Ahmed, S.A.1    McPhie, P.2    Smith, L.A.3
  • 26
    • 0037408049 scopus 로고    scopus 로고
    • Expression, purification, and efficacy of the type A botulinum neurotoxin catalytic domain fused to two translocation domain variants
    • Jensen, M. J., Smith, T. J., Ahmed, S. A., and Smith, L. A. (2003) Expression, purification, and efficacy of the type A botulinum neurotoxin catalytic domain fused to two translocation domain variants. Toxicon 41, 691-701
    • (2003) Toxicon , vol.41 , pp. 691-701
    • Jensen, M.J.1    Smith, T.J.2    Ahmed, S.A.3    Smith, L.A.4
  • 27
    • 33645411644 scopus 로고    scopus 로고
    • Expression, purification, and characterization of Clostridium botulinum type B light chain
    • Gilsdorf, J., Gul, N., and Smith, L. A. (2006) Expression, purification, and characterization of Clostridium botulinum type B light chain. Protein Expr. Purif. 46, 256-267
    • (2006) Protein Expr. Purif. , vol.46 , pp. 256-267
    • Gilsdorf, J.1    Gul, N.2    Smith, L.A.3
  • 28
    • 2342510157 scopus 로고    scopus 로고
    • Crystal structure of Clostridium botulinum neurotoxin protease in a product-bound state: Evidence for noncanonical zinc protease activity
    • Segelke, B., Knapp, M., Kadkhodayan, S., Balhorn, R., and Rupp, B. (2004) Crystal structure of Clostridium botulinum neurotoxin protease in a product-bound state: evidence for noncanonical zinc protease activity. Proc. Natl. Acad. Sci. U.S.A. 101, 6888-6893
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 6888-6893
    • Segelke, B.1    Knapp, M.2    Kadkhodayan, S.3    Balhorn, R.4    Rupp, B.5
  • 29
    • 45449096277 scopus 로고    scopus 로고
    • High level expression of the light chain of botulinum neurotoxin serotype C1 and an efficientHPLCassay to monitor its proteolytic activity
    • Rawat, R., Ashraf Ahmed, S., and Swaminathan, S. (2008) High level expression of the light chain of botulinum neurotoxin serotype C1 and an efficientHPLCassay to monitor its proteolytic activity. Protein Expr. Purif. 60, 165-169
    • (2008) Protein Expr. Purif. , vol.60 , pp. 165-169
    • Rawat, R.1    Ashraf Ahmed, S.2    Swaminathan, S.3
  • 30
    • 78751557157 scopus 로고    scopus 로고
    • Basic tetrapeptides as potent intracellular inhibitors of type A botulinum neurotoxin protease activity
    • Hale, M., Oyler, G., Swaminathan, S., and Ahmed, S. A. (2011) Basic tetrapeptides as potent intracellular inhibitors of type A botulinum neurotoxin protease activity. J. Biol. Chem. 286, 1802-1811
    • (2011) J. Biol. Chem. , vol.286 , pp. 1802-1811
    • Hale, M.1    Oyler, G.2    Swaminathan, S.3    Ahmed, S.A.4
  • 31
    • 0028558884 scopus 로고
    • Differences in the protease activities of tetanus and botulinum B toxins revealed by the cleavage of vesicle-associated membrane protein and various sized fragments
    • Foran, P., Shone, C. C., and Dolly, J. O. (1994) Differences in the protease activities of tetanus and botulinum B toxins revealed by the cleavage of vesicle-associated membrane protein and various sized fragments. Biochemistry 33, 15365-15374
    • (1994) Biochemistry , vol.33 , pp. 15365-15374
    • Foran, P.1    Shone, C.C.2    Dolly, J.O.3
  • 32
    • 70449704035 scopus 로고    scopus 로고
    • Rapid product analysis and increased sensitivity for quantitative determinations of botulinum neurotoxin proteolytic activity
    • Rowe, B., Schmidt, J. J., Smith, L. A., and Ahmed, S. A. (2010) Rapid product analysis and increased sensitivity for quantitative determinations of botulinum neurotoxin proteolytic activity. Anal. Biochem. 396, 188-193
    • (2010) Anal. Biochem. , vol.396 , pp. 188-193
    • Rowe, B.1    Schmidt, J.J.2    Smith, L.A.3    Ahmed, S.A.4
  • 33
    • 34248594822 scopus 로고    scopus 로고
    • Structures of Clostridium botulinum neurotoxin serotype A light chain complexed with small-molecule inhibitors highlight active-site flexibility
    • Silvaggi, N. R., Boldt, G. E., Hixon, M. S., Kennedy, J. P., Tzipori, S., Janda, K. D., and Allen, K. N. (2007) Structures of Clostridium botulinum neurotoxin serotype A light chain complexed with small-molecule inhibitors highlight active-site flexibility. Chem. Biol. 14, 533-542
    • (2007) Chem. Biol. , vol.14 , pp. 533-542
    • Silvaggi, N.R.1    Boldt, G.E.2    Hixon, M.S.3    Kennedy, J.P.4    Tzipori, S.5    Janda, K.D.6    Allen, K.N.7
  • 34
    • 79955851447 scopus 로고    scopus 로고
    • Structural characterization of three novel hydroxamate-based zinc chelating inhibitors of the Clostridium botulinum serotype A neurotoxin light chain metalloprotease reveals a compact binding site resulting from 60/70 loop flexibility
    • Thompson, A. A., Jiao, G. S., Kim, S., Thai, A., Cregar-Hernandez, L., Margosiak, S. A., Johnson, A. T., Han, G. W., O'Malley, S., and Stevens, R. C. (2011) Structural characterization of three novel hydroxamate-based zinc chelating inhibitors of the Clostridium botulinum serotype A neurotoxin light chain metalloprotease reveals a compact binding site resulting from 60/70 loop flexibility. Biochemistry 50, 4019-4028
    • (2011) Biochemistry , vol.50 , pp. 4019-4028
    • Thompson, A.A.1    Jiao, G.S.2    Kim, S.3    Thai, A.4    Cregar-Hernandez, L.5    Margosiak, S.A.6    Johnson, A.T.7    Han, G.W.8    O'Malley, S.9    Stevens, R.C.10
  • 35
    • 33744952947 scopus 로고    scopus 로고
    • Unique substrate recognition by botulinum neurotoxins serotypes A and e
    • Chen, S., and Barbieri, J. T. (2006) Unique substrate recognition by botulinum neurotoxins serotypes A and E. J. Biol. Chem. 281, 10906-10911
    • (2006) J. Biol. Chem. , vol.281 , pp. 10906-10911
    • Chen, S.1    Barbieri, J.T.2
  • 36
    • 0033520494 scopus 로고    scopus 로고
    • Sequence homology and structural analysis of the clostridial neurotoxins
    • Lacy, D. B., and Stevens, R. C. (1999) Sequence homology and structural analysis of the clostridial neurotoxins. J. Mol. Biol. 291, 1091-1104
    • (1999) J. Mol. Biol. , vol.291 , pp. 1091-1104
    • Lacy, D.B.1    Stevens, R.C.2
  • 37
    • 3242726206 scopus 로고    scopus 로고
    • Characterization of protein-protein interactions by isothermal titration calorimetry
    • Velazquez-Campoy, A., Leavitt, S. A., and Freire, E. (2004) Characterization of protein-protein interactions by isothermal titration calorimetry. Methods Mol. Biol. 261, 35-54
    • (2004) Methods Mol. Biol. , vol.261 , pp. 35-54
    • Velazquez-Campoy, A.1    Leavitt, S.A.2    Freire, E.3
  • 38
    • 68949124956 scopus 로고    scopus 로고
    • Extreme sensitivity of botulinum neurotoxin domains towards mild agitation
    • Toth, S. I., Smith, L. A., and Ahmed, S. A. (2009) Extreme sensitivity of botulinum neurotoxin domains towards mild agitation. J. Pharm. Sci. 98, 3302-3311
    • (2009) J. Pharm. Sci. , vol.98 , pp. 3302-3311
    • Toth, S.I.1    Smith, L.A.2    Ahmed, S.A.3
  • 39
    • 16244384489 scopus 로고    scopus 로고
    • Factors affecting autocatalysis of botulinum A neurotoxin light chain
    • Ahmed, S. A., Ludivico, M. L., and Smith, L. A. (2004) Factors affecting autocatalysis of botulinum A neurotoxin light chain. Protein J. 23, 445-451
    • (2004) Protein J. , vol.23 , pp. 445-451
    • Ahmed, S.A.1    Ludivico, M.L.2    Smith, L.A.3
  • 40
    • 0003692166 scopus 로고
    • 1st Ed The Benjamin/Cummings Publishing Co, Inc., Menlo Park CA
    • Mathews, C. K., and van Holde, K. E. (1990) in Biochemistry, 1st Ed., pp. 339-377 The Benjamin/Cummings Publishing Co, Inc., Menlo Park CA
    • (1990) Biochemistry , pp. 339-377
    • Mathews, C.K.1    Van Holde, K.E.2
  • 41
    • 0023664877 scopus 로고
    • Microcrystals of tryptophan synthase α2α2 complex from Salmonella typhimurium are catalytically active
    • Ahmed, S. A., Hyde, C. C., Thomas, G., and Miles, E. W. (1987) Microcrystals of tryptophan synthase α2α2 complex from Salmonella typhimurium are catalytically active. Biochemistry 26, 5492-5498
    • (1987) Biochemistry , vol.26 , pp. 5492-5498
    • Ahmed, S.A.1    Hyde, C.C.2    Thomas, G.3    Miles, E.W.4
  • 42
    • 0023058925 scopus 로고
    • Elimination of indole from L-tryptophan catalyzed by bacterial tryptophan synthase: A comparison between reactions catalyzed by tryptophanase and tryptophan synthase
    • Ahmed, S. A., Martin, B., and Miles, E. W. (1986)-Elimination of indole from L-tryptophan catalyzed by bacterial tryptophan synthase: a comparison between reactions catalyzed by tryptophanase and tryptophan synthase. Biochemistry 25, 4233-4240
    • (1986) Biochemistry , vol.25 , pp. 4233-4240
    • Ahmed, S.A.1    Martin, B.2    Miles, E.W.3
  • 43
    • 0035957229 scopus 로고    scopus 로고
    • Investigation of allosteric linkages in the regulation of tryptophan synthase: The roles of salt bridges and monovalent cations probed by site-directed mutation, optical spectroscopy, and kinetics
    • Weber-Ban, E., Hur, O., Bagwell, C., Banik, U., Yang, L. H., Miles, E. W., and Dunn, M. F. (2001) Investigation of allosteric linkages in the regulation of tryptophan synthase: the roles of salt bridges and monovalent cations probed by site-directed mutation, optical spectroscopy, and kinetics. Biochemistry 40, 3497-3511
    • (2001) Biochemistry , vol.40 , pp. 3497-3511
    • Weber-Ban, E.1    Hur, O.2    Bagwell, C.3    Banik, U.4    Yang, L.H.5    Miles, E.W.6    Dunn, M.F.7
  • 45
    • 0029613765 scopus 로고
    • Structure and function of tetanus and botulinum neurotoxins
    • Montecucco, C., and Schiavo, G. (1995) Structure and function of tetanus and botulinum neurotoxins. Q. Rev. Biophys. 28, 423-472
    • (1995) Q. Rev. Biophys. , vol.28 , pp. 423-472
    • Montecucco, C.1    Schiavo, G.2
  • 48
    • 1342323663 scopus 로고    scopus 로고
    • Identification of the major steps in botulinum toxin action
    • Simpson, L. L. (2004) Identification of the major steps in botulinum toxin action. Annu. Rev. Pharmacol. Toxicol. 44, 167-193
    • (2004) Annu. Rev. Pharmacol. Toxicol. , vol.44 , pp. 167-193
    • Simpson, L.L.1


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