메뉴 건너뛰기




Volumn 289, Issue 30, 2014, Pages 21131-21141

Allosteric activation of Bordetella pertussis Adenylyl cyclase by calmodulin: Molecular dynamics and mutagenesis studies

Author keywords

[No Author keywords available]

Indexed keywords

ADENYLATE CYCLASE TOXIN; BACTERIAL PROTEIN; CALMODULIN; MULTIPROTEIN COMPLEX;

EID: 84905375146     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.530410     Document Type: Article
Times cited : (17)

References (50)
  • 1
    • 0032586774 scopus 로고    scopus 로고
    • Bordetella pertussis adenylate cyclase: A toxin with multiple talents
    • Ladant, D., and Ullmann, A. (1999) Bordetella pertussis adenylate cyclase: a toxin with multiple talents. Trends Microbiol. 7, 172-176
    • (1999) Trends Microbiol. , vol.7 , pp. 172-176
    • Ladant, D.1    Ullmann, A.2
  • 2
    • 31844435261 scopus 로고    scopus 로고
    • Bordetella adenylate cyclase toxin: A swift saboteur of host defense
    • Vojtova, J., Kamanova, J., and Sebo, P. (2006) Bordetella adenylate cyclase toxin: a swift saboteur of host defense. Curr. Opin. Microbiol. 9, 69-75
    • (2006) Curr. Opin. Microbiol. , vol.9 , pp. 69-75
    • Vojtova, J.1    Kamanova, J.2    Sebo, P.3
  • 3
    • 77949345512 scopus 로고    scopus 로고
    • Pertussis toxin and adenylate cyclase toxin: Key virulence factors of Bordetella pertussis and cell biology tools
    • Carbonetti, N. (2010) Pertussis toxin and adenylate cyclase toxin: key virulence factors of Bordetella pertussis and cell biology tools. Future Microbiol. 5, 455-469
    • (2010) Future Microbiol. , vol.5 , pp. 455-469
    • Carbonetti, N.1
  • 5
    • 0019973678 scopus 로고
    • Phagocyte impotence caused by an invasive bacterial adenylate cyclase
    • Confer, D. L., and Eaton, J. W. (1982) Phagocyte impotence caused by an invasive bacterial adenylate cyclase. Science 217, 948-950
    • (1982) Science , vol.217 , pp. 948-950
    • Confer, D.L.1    Eaton, J.W.2
  • 6
    • 0024449602 scopus 로고
    • Bordetella pertussis adenylate cyclase: Purification and characterization of the toxic form of the enzyme
    • Rogel, A., Schultz, J. E., Brownlie, R. M., Coote, J. G., Parton, R., and Hanski, E. (1989) Bordetella pertussis adenylate cyclase: purification and characterization of the toxic form of the enzyme. EMBO J. 8, 2755-2760
    • (1989) EMBO J. , vol.8 , pp. 2755-2760
    • Rogel, A.1    Schultz, J.E.2    Brownlie, R.M.3    Coote, J.G.4    Parton, R.5    Hanski, E.6
  • 7
    • 0025162502 scopus 로고
    • Adenylate cyclase toxin is critical for colonization, and pertussis toxin is critical for lethal infection by Bordetella pertussis in infant mice
    • Goodwin, M., and Weiss, A. A. (1990) Adenylate cyclase toxin is critical for colonization, and pertussis toxin is critical for lethal infection by Bordetella pertussis in infant mice. Infect. Immun. 58, 3445-3447
    • (1990) Infect. Immun. , vol.58 , pp. 3445-3447
    • Goodwin, M.1    Weiss, A.A.2
  • 8
    • 0027374664 scopus 로고
    • Bordetella pertussis induces apoptosis in macrophages: Role of adenylate cyclase-hemolysin
    • Khelef, N., Zychlinsky, A., and Guiso, N. (1993) Bordetella pertussis induces apoptosis in macrophages: role of adenylate cyclase-hemolysin. Infect. Immun. 61, 4064-4071
    • (1993) Infect. Immun. , vol.61 , pp. 4064-4071
    • Khelef, N.1    Zychlinsky, A.2    Guiso, N.3
  • 9
    • 0032976371 scopus 로고    scopus 로고
    • Probing the function of Bordetella bronchiseptica adenylate cyclase toxin by manipulating host immunity
    • Harvill, E. T., Cotter, P. A., Yuk, M. H., and Miller, J. F. (1999) Probing the function of Bordetella bronchiseptica adenylate cyclase toxin by manipulating host immunity. Infect. Immun. 67, 1493-1500
    • (1999) Infect. Immun. , vol.67 , pp. 1493-1500
    • Harvill, E.T.1    Cotter, P.A.2    Yuk, M.H.3    Miller, J.F.4
  • 10
    • 33645050136 scopus 로고    scopus 로고
    • Macrophage cytotoxicity produced by adenylate cyclase toxin from Bordetella pertussis: More than just making cyclic AMP!
    • Hewlett, E. L., Donato, G. M., and Gray, M. C. (2006) Macrophage cytotoxicity produced by adenylate cyclase toxin from Bordetella pertussis: more than just making cyclic AMP!. Mol. Microbiol. 59, 447-459
    • (2006) Mol. Microbiol. , vol.59 , pp. 447-459
    • Hewlett, E.L.1    Donato, G.M.2    Gray, M.C.3
  • 11
    • 37049038863 scopus 로고    scopus 로고
    • Transcriptional responses of murine macrophages to the adenylate cyclase toxin of Bordetella pertussis
    • Cheung, G. Y., Dickinson, P., Sing, G., Craigon, M., Ghazal, P., Parton, R., and Coote, J. G. (2008) Transcriptional responses of murine macrophages to the adenylate cyclase toxin of Bordetella pertussis. Microb. Pathog. 44, 61-70
    • (2008) Microb. Pathog. , vol.44 , pp. 61-70
    • Cheung, G.Y.1    Dickinson, P.2    Sing, G.3    Craigon, M.4    Ghazal, P.5    Parton, R.6    Coote, J.G.7
  • 13
    • 25144469471 scopus 로고    scopus 로고
    • Structural basis for the interaction of Bordetella pertussis adenylyl cyclase toxin with calmodulin
    • Guo, Q., Shen, Y., Lee, Y. S., Gibbs, C. S., Mrksich, M., and Tang, W. J. (2005) Structural basis for the interaction of Bordetella pertussis adenylyl cyclase toxin with calmodulin. EMBO J. 24, 3190-3201
    • (2005) EMBO J. , vol.24 , pp. 3190-3201
    • Guo, Q.1    Shen, Y.2    Lee, Y.S.3    Gibbs, C.S.4    Mrksich, M.5    Tang, W.J.6
  • 15
    • 84857781698 scopus 로고    scopus 로고
    • Differential role of calmodulin and calcium ions in the stabilization of the catalytic domain of adenyl cyclase CyaA from Bordetella pertussis
    • Selwa, E., Laine, E., and Malliavin, T. (2012) Differential role of calmodulin and calcium ions in the stabilization of the catalytic domain of adenyl cyclase CyaA from Bordetella pertussis. Proteins 80, 1028-1040
    • (2012) Proteins , vol.80 , pp. 1028-1040
    • Selwa, E.1    Laine, E.2    Malliavin, T.3
  • 16
    • 33645779767 scopus 로고    scopus 로고
    • Dependency map of proteins in the small ribosomal subunit
    • Hamacher, K., Trylska, J., and McCammon, J. (2006) Dependency map of proteins in the small ribosomal subunit. PloS Comput. Biol. 2, e10
    • (2006) PloS Comput. Biol. , vol.2
    • Hamacher, K.1    Trylska, J.2    McCammon, J.3
  • 17
    • 62649096330 scopus 로고    scopus 로고
    • Dynamics and energetics: A consensus analysis of the impact of calcium on EF-CaM protein complex
    • Laine, E., Blondel, A., and Malliavin, T. (2009) Dynamics and energetics: a consensus analysis of the impact of calcium on EF-CaM protein complex. Biophys. J. 96, 1249-1263
    • (2009) Biophys. J. , vol.96 , pp. 1249-1263
    • Laine, E.1    Blondel, A.2    Malliavin, T.3
  • 19
    • 33748518255 scopus 로고    scopus 로고
    • Comparison of multiple AMBER force fields and development of improved protein backbone parameters
    • Hornak, V., Abel, R., Okur, A., Strockbine, B., Roitberg, A., and Simmerling, C. (2006) Comparison of multiple AMBER force fields and development of improved protein backbone parameters. Proteins 65, 712-725
    • (2006) Proteins , vol.65 , pp. 712-725
    • Hornak, V.1    Abel, R.2    Okur, A.3    Strockbine, B.4    Roitberg, A.5    Simmerling, C.6
  • 20
    • 33645858780 scopus 로고
    • Quantum and statistical mechanical studies of liquids. 10. Transferable intermolecular potential functions for water, alcohols, and ethers. Application to liquid water
    • Jorgensen, W. (1981) Quantum and statistical mechanical studies of liquids. 10. Transferable intermolecular potential functions for water, alcohols, and ethers. Application to liquid water. J. Am. Chem. Soc. 103, 335-340
    • (1981) J. Am. Chem. Soc. , vol.103 , pp. 335-340
    • Jorgensen, W.1
  • 21
    • 0344796204 scopus 로고
    • Ion-water interaction potentials derived from free energy perturbation simulations
    • Aqvist, J. (1990) Ion-water interaction potentials derived from free energy perturbation simulations. J. Phys. Chem. 94, 8021-8024
    • (1990) J. Phys. Chem. , vol.94 , pp. 8021-8024
    • Aqvist, J.1
  • 22
    • 34147192127 scopus 로고    scopus 로고
    • Biskit: A software platform for structural bioinformatics
    • Grünberg, R., Nilges, M., and Leckner, J. (2007) Biskit: a software platform for structural bioinformatics. Bioinformatics 23, 769-770
    • (2007) Bioinformatics , vol.23 , pp. 769-770
    • Grünberg, R.1    Nilges, M.2    Leckner, J.3
  • 23
    • 84872012970 scopus 로고    scopus 로고
    • Molecular mechanism of allosteric communication in Hsp70 revealed by molecular dynamics simulations
    • Chiappori, F., Merelli, I., Colombo, G., Milanesi, L., and Morra, G. (2012) Molecular mechanism of allosteric communication in Hsp70 revealed by molecular dynamics simulations. PLoS Comput. Biol. 8, e1002844
    • (2012) PLoS Comput. Biol. , vol.8
    • Chiappori, F.1    Merelli, I.2    Colombo, G.3    Milanesi, L.4    Morra, G.5
  • 24
    • 3142661063 scopus 로고    scopus 로고
    • Essential role of methionine residues in calmodulin binding to Bordetella pertussis adenylate cyclase, as probed by selective oxidation and repair by the peptide methionine sulfoxide reductases
    • Vougier, S., Mary, J., Dautin, N., Vinh, J., Friguet, B., and Ladant, D. (2004) Essential role of methionine residues in calmodulin binding to Bordetella pertussis adenylate cyclase, as probed by selective oxidation and repair by the peptide methionine sulfoxide reductases. J. Biol. Chem. 279, 30210-30218
    • (2004) J. Biol. Chem. , vol.279 , pp. 30210-30218
    • Vougier, S.1    Mary, J.2    Dautin, N.3    Vinh, J.4    Friguet, B.5    Ladant, D.6
  • 25
    • 0034756154 scopus 로고    scopus 로고
    • Characterization of recombinant Bordetella pertussis adenylate cyclase toxins carrying passenger proteins
    • Gmira, S., Karimova, G., and Ladant, D. (2001) Characterization of recombinant Bordetella pertussis adenylate cyclase toxins carrying passenger proteins. Res. Microbiol. 152, 889-900
    • (2001) Res. Microbiol. , vol.152 , pp. 889-900
    • Gmira, S.1    Karimova, G.2    Ladant, D.3
  • 26
    • 0035151432 scopus 로고    scopus 로고
    • Protein-protein interaction between Bacillus stearothermophilus tyrosyl-tRNA synthetase subdomains revealed by a bacterial two-hybrid system
    • Karimova, G., Ullmann, A., and Ladant, D. (2001) Protein-protein interaction between Bacillus stearothermophilus tyrosyl-tRNA synthetase subdomains revealed by a bacterial two-hybrid system. J. Mol. Microbiol. Biotechnol. 3, 73-82
    • (2001) J. Mol. Microbiol. Biotechnol. , vol.3 , pp. 73-82
    • Karimova, G.1    Ullmann, A.2    Ladant, D.3
  • 28
    • 75349096080 scopus 로고    scopus 로고
    • Calmodulin-induced conformational and hydrodynamic changes in the catalytic domain of Bordetella pertussis adenylate cyclase toxin
    • Karst, J. C., Sotomayor-Pérez, A. C., Guijarro, J. I., Raynal, B., Chenal, A., and Ladant, D. (2010) Calmodulin-induced conformational and hydrodynamic changes in the catalytic domain of Bordetella pertussis adenylate cyclase toxin. Biochemistry 49, 318-328
    • (2010) Biochemistry , vol.49 , pp. 318-328
    • Karst, J.C.1    Sotomayor-Pérez, A.C.2    Guijarro, J.I.3    Raynal, B.4    Chenal, A.5    Ladant, D.6
  • 29
    • 84882248932 scopus 로고    scopus 로고
    • Molecular crowding stabilizes both the intrinsically disordered calciumfree state and the folded calcium-bound state of a repeat in toxin (RTX) protein
    • Sotomayor-Pérez, A. C., Subrini, O., Hessel, A., Ladant, D., and Chenal, A. (2013) Molecular crowding stabilizes both the intrinsically disordered calciumfree state and the folded calcium-bound state of a repeat in toxin (RTX) protein. J. Am. Chem. Soc. 135, 11929-11934
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 11929-11934
    • Sotomayor-Pérez, A.C.1    Subrini, O.2    Hessel, A.3    Ladant, D.4    Chenal, A.5
  • 30
    • 78649896548 scopus 로고    scopus 로고
    • Calcium-induced folding and stabilization of the intrinsically disordered RTX domain of the CyaA toxin
    • Chenal, A., Karst, J. C., Sotomayor-Pérez, A. C., Wozniak, A. K., Baron, B., England, P., and Ladant, D. (2010) Calcium-induced folding and stabilization of the intrinsically disordered RTX domain of the CyaA toxin. Biophys. J. 99, 3744-3753
    • (2010) Biophys. J. , vol.99 , pp. 3744-3753
    • Chenal, A.1    Karst, J.C.2    Sotomayor-Pérez, A.C.3    Wozniak, A.K.4    Baron, B.5    England, P.6    Ladant, D.7
  • 31
    • 41449103543 scopus 로고    scopus 로고
    • 2+ dissociation from the C-terminal EF-hand pair in calmodulin: A steered molecular dynamics study
    • 2+ dissociation from the C-terminal EF-hand pair in calmodulin: a steered molecular dynamics study. FEBS Lett. 582, 1355-1361
    • (2008) FEBS Lett. , vol.582 , pp. 1355-1361
    • Zhang, Y.1    Tan, H.2    Lu, Y.3    Jia, Z.4    Chen, G.5
  • 32
    • 0029160568 scopus 로고
    • Calcium-induced conformational transition revealed by the solution structure of apo calmodulin
    • Zhang, M., Tanaka, T., and Ikura, M. (1995) Calcium-induced conformational transition revealed by the solution structure of apo calmodulin. Nat. Struct. Biol. 2, 758-767
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 758-767
    • Zhang, M.1    Tanaka, T.2    Ikura, M.3
  • 34
    • 0024447834 scopus 로고
    • Identification of residues essential for catalysis and binding of calmodulin in Bordetella pertussis adenylate cyclase by sitedirected mutagenesis
    • Glaser, P., Elmaoglou-Lazaridou, A., Krin, E., Ladant, D., Bârzu, O., and Danchin, A. (1989) Identification of residues essential for catalysis and binding of calmodulin in Bordetella pertussis adenylate cyclase by sitedirected mutagenesis. EMBO J. 8, 967-972
    • (1989) EMBO J. , vol.8 , pp. 967-972
    • Glaser, P.1    Elmaoglou-Lazaridou, A.2    Krin, E.3    Ladant, D.4    Bârzu, O.5    Danchin, A.6
  • 35
    • 84859455527 scopus 로고    scopus 로고
    • Structure-based model of allostery predicts coupling between distant sites
    • Weinkam, P., Pons, J., and Sali, A. (2012) Structure-based model of allostery predicts coupling between distant sites. Proc. Natl. Acad. Sci. U. S. A. 109, 4875-4880
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , pp. 4875-4880
    • Weinkam, P.1    Pons, J.2    Sali, A.3
  • 36
    • 84872835595 scopus 로고    scopus 로고
    • Impact of mutations on the allosteric conformational equilibrium
    • Weinkam, P., Chen, Y. C., Pons, J., and Sali, A. (2013) Impact of mutations on the allosteric conformational equilibrium. J. Mol. Biol. 425, 647-661
    • (2013) J. Mol. Biol. , vol.425 , pp. 647-661
    • Weinkam, P.1    Chen, Y.C.2    Pons, J.3    Sali, A.4
  • 37
    • 34848882812 scopus 로고    scopus 로고
    • Signal propagation in proteins and relation to equilibrium fluctuations
    • Chennubhotla, C., and Bahar, I. (2007) Signal propagation in proteins and relation to equilibrium fluctuations. PLoS Comput. Biol. 3, 1716-1726
    • (2007) PLoS Comput. Biol. , vol.3 , pp. 1716-1726
    • Chennubhotla, C.1    Bahar, I.2
  • 38
    • 68149157248 scopus 로고    scopus 로고
    • The origin of allosteric functional modulation: Multiple pre-existing pathways
    • del Sol, A., Tsai, C. J., Ma, B., and Nussinov, R. (2009) The origin of allosteric functional modulation: multiple pre-existing pathways. Structure 17, 1042-1050
    • (2009) Structure , vol.17 , pp. 1042-1050
    • Del Sol, A.1    Tsai, C.J.2    Ma, B.3    Nussinov, R.4
  • 39
    • 80053443092 scopus 로고    scopus 로고
    • Long-range intraprotein communication can be transmitted by correlated side-chain fluctuations alone
    • Dubay, K. H., Bothma, J. P., and Geissler, P. L. (2011) Long-range intraprotein communication can be transmitted by correlated side-chain fluctuations alone. PLoS Comput. Biol. 7, e1002168
    • (2011) PLoS Comput. Biol. , vol.7
    • Dubay, K.H.1    Bothma, J.P.2    Geissler, P.L.3
  • 40
    • 84862625522 scopus 로고    scopus 로고
    • Constructing structural networks of signaling pathways on the proteome scale
    • Kuzu, G., Keskin, O., Gursoy, A., and Nussinov, R. (2012) Constructing structural networks of signaling pathways on the proteome scale. Curr. Opin. Struct. Biol. 22, 367-377
    • (2012) Curr. Opin. Struct. Biol. , vol.22 , pp. 367-377
    • Kuzu, G.1    Keskin, O.2    Gursoy, A.3    Nussinov, R.4
  • 41
    • 84870707533 scopus 로고    scopus 로고
    • Accurate prediction of the dynamical changes within the second PDZ domain of PTP1e
    • Cilia, E., Vuister, G. W., and Lenaerts, T. (2012) Accurate prediction of the dynamical changes within the second PDZ domain of PTP1e. PLoS Comput. Biol. 8, e1002794
    • (2012) PLoS Comput. Biol. , vol.8
    • Cilia, E.1    Vuister, G.W.2    Lenaerts, T.3
  • 42
    • 70149090164 scopus 로고    scopus 로고
    • The intrinsic dynamics of enzymes plays a dominant role in determining the structural changes induced upon inhibitor binding
    • Bakan, A., and Bahar, I. (2009) The intrinsic dynamics of enzymes plays a dominant role in determining the structural changes induced upon inhibitor binding. Proc. Natl. Acad. Sci. U. S. A. 106, 14349-14354
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 14349-14354
    • Bakan, A.1    Bahar, I.2
  • 43
    • 84883480131 scopus 로고    scopus 로고
    • Allosteric conformational barcodes direct signaling in the cell
    • Nussinov, R., Ma, B., Tsai, C. J., and Csermely, P. (2013) Allosteric conformational barcodes direct signaling in the cell. Structure 21, 1509-1521
    • (2013) Structure , vol.21 , pp. 1509-1521
    • Nussinov, R.1    Ma, B.2    Tsai, C.J.3    Csermely, P.4
  • 44
    • 0033536602 scopus 로고    scopus 로고
    • Evolutionarily conserved pathways of energetic connectivity in protein families
    • Lockless, S. W., and Ranganathan, R. (1999) Evolutionarily conserved pathways of energetic connectivity in protein families. Science 286, 295-299
    • (1999) Science , vol.286 , pp. 295-299
    • Lockless, S.W.1    Ranganathan, R.2
  • 45
    • 77955330195 scopus 로고    scopus 로고
    • Identifying and seeing beyond multiple sequence alignment errors using intra-molecular protein covariation
    • Dickson, R. J., Wahl, L. M., Fernandes, A. D., and Gloor, G. B. (2010) Identifying and seeing beyond multiple sequence alignment errors using intra-molecular protein covariation. PLoS One 5, e11082
    • (2010) PLoS One , vol.5
    • Dickson, R.J.1    Wahl, L.M.2    Fernandes, A.D.3    Gloor, G.B.4
  • 46
    • 84455167671 scopus 로고    scopus 로고
    • Hot spots for allosteric regulation on protein surfaces
    • Reynolds, K. A., McLaughlin, R. N., and Ranganathan, R. (2011) Hot spots for allosteric regulation on protein surfaces. Cell 147, 1564-1575
    • (2011) Cell , vol.147 , pp. 1564-1575
    • Reynolds, K.A.1    McLaughlin, R.N.2    Ranganathan, R.3
  • 49
    • 84862760801 scopus 로고    scopus 로고
    • Towards selective inhibitors of adenylyl cyclase toxin from Bordetella pertussis
    • Seifert, R., and Dove, S. (2012) Towards selective inhibitors of adenylyl cyclase toxin from Bordetella pertussis. Trends Microbiol. 20, 343-351
    • (2012) Trends Microbiol. , vol.20 , pp. 343-351
    • Seifert, R.1    Dove, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.