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Volumn 30, Issue 4, 1998, Pages 442-454

Crystallographic and spectroscopic characterization of a molecular hinge: Conformational changes in Bothropstoxin I, a dimeric Lys49- phospholipase A2 homologue

Author keywords

Protein membrane interaction; Quaternary structural change; Spectroscopy; Venom toxin; X ray diffraction

Indexed keywords

DIMER; LYSINE; MONOMER; PHOSPHOLIPASE A2; SNAKE VENOM; TRYPTOPHAN;

EID: 0032031373     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(19980301)30:4<442::AID-PROT11>3.0.CO;2-I     Document Type: Article
Times cited : (102)

References (57)
  • 1
    • 0000498403 scopus 로고
    • The phospholipases
    • Hanahan, D.J. (ed.). New York: Plenum Press
    • Waite, M. The phospholipases. In: "Handbook of Lipid Research Vol. 5." Hanahan, D.J. (ed.). New York: Plenum Press, 1987.
    • (1987) Handbook of Lipid Research , vol.5
    • Waite, M.1
  • 2
    • 0025827082 scopus 로고
    • Dissection and sequence analysis of phospholipase A2
    • Heinrikson, R.L. Dissection and sequence analysis of phospholipase A2. Methods Enzymol. 197:201-215, 1990.
    • (1990) Methods Enzymol. , vol.197 , pp. 201-215
    • Heinrikson, R.L.1
  • 3
    • 0028338536 scopus 로고
    • Diversity of group types, regulation, and function of phospholipase A2
    • Dennis, E.A. Diversity of group types, regulation, and function of phospholipase A2. J. Biol. Chem. 269:13057-13060, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 13057-13060
    • Dennis, E.A.1
  • 4
    • 0028169417 scopus 로고
    • Phospholipase A2 enzymes: Regulation and physiological role
    • Mukherjee, A.B., Miele, L., Pattabiraman, N. Phospholipase A2 enzymes: Regulation and physiological role. Biochem. Pharmacol. 48:1-10, 1994.
    • (1994) Biochem. Pharmacol. , vol.48 , pp. 1-10
    • Mukherjee, A.B.1    Miele, L.2    Pattabiraman, N.3
  • 6
    • 0000311077 scopus 로고
    • The relationship between enzymatic activity and pharmacological properties of phospholipases in natural poisons
    • Harris, J.B. (ed.). Oxford: Clarendon Press
    • Rosenberg, P.R. The relationship between enzymatic activity and pharmacological properties of phospholipases in natural poisons. In: "Natural Toxins." Harris, J.B. (ed.). Oxford: Clarendon Press, 1986:129-174.
    • (1986) Natural Toxins , pp. 129-174
    • Rosenberg, P.R.1
  • 7
    • 0023006079 scopus 로고
    • Myotoxic activity of phospholipase A2 isolated from cobra venoms: Neutralization by polyvalent antivenoms
    • Mebs, D. Myotoxic activity of phospholipase A2 isolated from cobra venoms: Neutralization by polyvalent antivenoms Toxicon 24:161-168, 1986.
    • (1986) Toxicon , vol.24 , pp. 161-168
    • Mebs, D.1
  • 8
    • 0028972997 scopus 로고
    • Phospholipase A2 myotoxins from Bothrops snake venoms
    • Gutiérrez, J.M., Lomonte, B. Phospholipase A2 myotoxins from Bothrops snake venoms. Toxicon 33:1405-1424, 1995.
    • (1995) Toxicon , vol.33 , pp. 1405-1424
    • Gutiérrez, J.M.1    Lomonte, B.2
  • 9
    • 0027232904 scopus 로고
    • Purification and characterization of a snake venom phospholipase A2: A potent inhibitor of platelet aggregation
    • Yuan, Y., Jackson, S.P., Mitchell, C.A., Salem, H.H. Purification and characterization of a snake venom phospholipase A2: A potent inhibitor of platelet aggregation. Thromb. Res. 70:471-481, 1993.
    • (1993) Thromb. Res. , vol.70 , pp. 471-481
    • Yuan, Y.1    Jackson, S.P.2    Mitchell, C.A.3    Salem, H.H.4
  • 10
    • 0027665462 scopus 로고
    • Increased phosphatidic acid and decreased lysophosphatidic acid in response to thrombin is associated with inhibition of platelet aggregation
    • Gerard, J.M., Robinson, P., Narvey, M., McNicol, A. Increased phosphatidic acid and decreased lysophosphatidic acid in response to thrombin is associated with inhibition of platelet aggregation. Biochem. Cell. Biol. 71:432-439, 1993.
    • (1993) Biochem. Cell. Biol. , vol.71 , pp. 432-439
    • Gerard, J.M.1    Robinson, P.2    Narvey, M.3    McNicol, A.4
  • 11
    • 0017355161 scopus 로고
    • The presynaptic nueromuscular blocking action of taipoxin. A comparison with β-bungarotoxin and crotoxin
    • Chang, C.C., Lee, C.Y., Eaker, D., Fohlman, J. The presynaptic nueromuscular blocking action of taipoxin. A comparison with β-bungarotoxin and crotoxin. Toxicon 15:571-576, 1977.
    • (1977) Toxicon , vol.15 , pp. 571-576
    • Chang, C.C.1    Lee, C.Y.2    Eaker, D.3    Fohlman, J.4
  • 14
    • 0028920873 scopus 로고
    • Kinetic basis for interfacial catalysis by phospholipase A2
    • Jain, M.K., Gelb, M.H., Rogers, J., Berg, O.G. Kinetic basis for interfacial catalysis by phospholipase A2. Methods Enzymol. 249:567-614, 1995.
    • (1995) Methods Enzymol. , vol.249 , pp. 567-614
    • Jain, M.K.1    Gelb, M.H.2    Rogers, J.3    Berg, O.G.4
  • 15
    • 0025668794 scopus 로고
    • Crystal structure of bee-venom phospholipase A2 in a complex with a transition state analogue
    • Scott, D.L., Otwinowski, Z., Gelb, H.G., Sigler, P.B. Crystal structure of bee-venom phospholipase A2 in a complex with a transition state analogue. Science 250:1563-1566, 1990.
    • (1990) Science , vol.250 , pp. 1563-1566
    • Scott, D.L.1    Otwinowski, Z.2    Gelb, H.G.3    Sigler, P.B.4
  • 17
    • 0028358009 scopus 로고
    • Structure and catalytic mechanism of secretory phospholipases A2
    • Scott, D.L., Sigler, P.B. Structure and catalytic mechanism of secretory phospholipases A2. Adv. Protein Chem. 45:53-88, 1994.
    • (1994) Adv. Protein Chem. , vol.45 , pp. 53-88
    • Scott, D.L.1    Sigler, P.B.2
  • 19
    • 0026499354 scopus 로고
    • Crystallographic and biochemical studies of the (inactive) Lys-49 phospholipase A2 from the venom of Agkistrodon piscivorus piscivorus
    • Scott, D.L., Achari, A., Vidal, J.C., Sigler, P.B. Crystallographic and biochemical studies of the (inactive) Lys-49 phospholipase A2 from the venom of Agkistrodon piscivorus piscivorus. J. Biol. Chem. 267:22645-22657, 1992.
    • (1992) J. Biol. Chem. , vol.267 , pp. 22645-22657
    • Scott, D.L.1    Achari, A.2    Vidal, J.C.3    Sigler, P.B.4
  • 20
    • 0029124677 scopus 로고
    • Structure of a calcium independent phospholipase-like myotoxic protein from Bothrops asper venom
    • Arni, R.K., Ward, R.J., Gutierrez, J.M., Tulinsky, A. Structure of a calcium independent phospholipase-like myotoxic protein from Bothrops asper venom. Acta. Cryst. D51:311-317, 1995.
    • (1995) Acta. Cryst. , vol.D51 , pp. 311-317
    • Arni, R.K.1    Ward, R.J.2    Gutierrez, J.M.3    Tulinsky, A.4
  • 21
    • 0028670213 scopus 로고
    • Phospholipase A2 engineering. Structural and functional roles of the highly conserved active site residue aspartate-49
    • Li, Y., Yu, B-Z., Zhu, H., Jain, M.K., Tsai, M-D. Phospholipase A2 engineering. Structural and functional roles of the highly conserved active site residue aspartate-49. Biochemistry 33:14714-14722, 1994.
    • (1994) Biochemistry , vol.33 , pp. 14714-14722
    • Li, Y.1    Yu, B.-Z.2    Zhu, H.3    Jain, M.K.4    Tsai, M.-D.5
  • 22
    • 0024654781 scopus 로고
    • The role of Asp-49 and other conserved amino acids in phospholipases A2 and their importance for enzymatic activity
    • Van den Bergh, C.J., Slotboom, A.J., Verheij, H.M., de Haas, G.H. The role of Asp-49 and other conserved amino acids in phospholipases A2 and their importance for enzymatic activity. J. Cell. Biochem. 39:379-390, 1989.
    • (1989) J. Cell. Biochem. , vol.39 , pp. 379-390
    • Van Den Bergh, C.J.1    Slotboom, A.J.2    Verheij, H.M.3    De Haas, G.H.4
  • 23
    • 0026068009 scopus 로고
    • The effect of myotoxins isolated from Bothrops snake venoms on multilamellar liposomes: Relationship to phospholipase A2, anticoagulant and myotoxic activities
    • Díaz, C., Gutiérrez, J.M., Lomonte, B. Gene, J.A. The effect of myotoxins isolated from Bothrops snake venoms on multilamellar liposomes: Relationship to phospholipase A2, anticoagulant and myotoxic activities. Biochem. Biophys. Acta 1070:455-460, 1991.
    • (1991) Biochem. Biophys. Acta , vol.1070 , pp. 455-460
    • Díaz, C.1    Gutiérrez, J.M.2    Lomonte, B.3    Gene, J.A.4
  • 25
    • 0022467432 scopus 로고
    • Pharamcological activities of a toxic phospholipase A isolated from the venom of the snake Bothrops asper
    • Gutiérrez, J.M., Lomonte, B., Chaves, F., Moreno, E., Cerdas, L. Pharamcological activities of a toxic phospholipase A isolated from the venom of the snake Bothrops asper. Comp. Biochem. Physiol. 84C:159-164, 1986.
    • (1986) Comp. Biochem. Physiol. , vol.84 C , pp. 159-164
    • Gutiérrez, J.M.1    Lomonte, B.2    Chaves, F.3    Moreno, E.4    Cerdas, L.5
  • 26
    • 0027509737 scopus 로고
    • Specific in vitro biological activity of snake venom myotoxins
    • Brusés, J.L., Capaso, J., Katz, T., Pilar, G. Specific in vitro biological activity of snake venom myotoxins. J. Neurochem. 60:1030-1042, 1993.
    • (1993) J. Neurochem. , vol.60 , pp. 1030-1042
    • Brusés, J.L.1    Capaso, J.2    Katz, T.3    Pilar, G.4
  • 27
    • 0028113348 scopus 로고
    • Broad cytolytic specificity of myotoxin II, a Lysine-49 phospholipase A2 of Bothrops asper snake venom
    • Lomonte, B., Tarkowski, A. Hanson, L.A. Broad cytolytic specificity of myotoxin II, a Lysine-49 phospholipase A2 of Bothrops asper snake venom. Toxicon 32:1359-1369, 1994.
    • (1994) Toxicon , vol.32 , pp. 1359-1369
    • Lomonte, B.1    Tarkowski, A.2    Hanson, L.A.3
  • 28
    • 0028040204 scopus 로고
    • Phospholipase-like myotoxins induce rapid membrane leakage of non-hydrolyzable ether-lipid liposomes
    • Pedersen, J.Z., de Arcuri, B.F., Moreno, R.D., Rufini, S. Phospholipase-like myotoxins induce rapid membrane leakage of non-hydrolyzable ether-lipid liposomes. Biochem. Biophys. Acta. 1190:177-180, 1994.
    • (1994) Biochem. Biophys. Acta , vol.1190 , pp. 177-180
    • Pedersen, J.Z.1    De Arcuri, B.F.2    Moreno, R.D.3    Rufini, S.4
  • 29
    • 0024412266 scopus 로고
    • A new muscle damaging toxin, myotoxin II, from the venom of the snake Bothrops asper (terciopelo)
    • Lomonte, B. Gutiérrez, J.M. A new muscle damaging toxin, myotoxin II, from the venom of the snake Bothrops asper (terciopelo). Toxicon 27:725-733, 1989.
    • (1989) Toxicon , vol.27 , pp. 725-733
    • Lomonte, B.1    Gutiérrez, J.M.2
  • 30
    • 0023878851 scopus 로고
    • Fractionation of Bothrops jararacussu snake venom: Partial chemical characterization and biological activity of Bothropstoxin
    • Homsi-Brandenburgo M.I., Queiroz L.S., Santo-Neto H., Rodrigues-Simioni L., Giglio J.R. Fractionation of Bothrops jararacussu snake venom: Partial chemical characterization and biological activity of Bothropstoxin. Toxicon 26:615-627, 1988.
    • (1988) Toxicon , vol.26 , pp. 615-627
    • Homsi-Brandenburgo, M.I.1    Queiroz, L.S.2    Santo-Neto, H.3    Rodrigues-Simioni, L.4    Giglio, J.R.5
  • 32
    • 0028986763 scopus 로고
    • Nucleotide sequence of a cDNA encoding bothropstoxin I, a myotoxin from the venom of Bothrops jararacussu
    • Ward, R.J., Monesi, N., Arni, R.K., Larson, R.E., Paço-Larson, M.L. Nucleotide sequence of a cDNA encoding bothropstoxin I, a myotoxin from the venom of Bothrops jararacussu. Gene 156:305-306, 1995.
    • (1995) Gene , vol.156 , pp. 305-306
    • Ward, R.J.1    Monesi, N.2    Arni, R.K.3    Larson, R.E.4    Paço-Larson, M.L.5
  • 33
    • 0025959248 scopus 로고
    • Myotoxin II from Bothrops asper (terciopelo) venom is a lysine-49 phospholipase A2
    • Francis, B., Gutiérrez, J.M., Lomonte, B., Kaiser, I.I. Myotoxin II from Bothrops asper (terciopelo) venom is a lysine-49 phospholipase A2. Arch. Biochem. Biophys. 284: 352-359, 1991.
    • (1991) Arch. Biochem. Biophys. , vol.284 , pp. 352-359
    • Francis, B.1    Gutiérrez, J.M.2    Lomonte, B.3    Kaiser, I.I.4
  • 35
    • 0027164733 scopus 로고
    • Crystallization and preliminary diffraction data of two miotoxins isolated from the venoms of Bothrops asper (terciopelo) and Bothrops nummifer (jumping viper)
    • Arni, R.K., Gutiérrez, J.M. Crystallization and preliminary diffraction data of two miotoxins isolated from the venoms of Bothrops asper (terciopelo) and Bothrops nummifer (jumping viper). Toxicon 31:1061-1064, 1993.
    • (1993) Toxicon , vol.31 , pp. 1061-1064
    • Arni, R.K.1    Gutiérrez, J.M.2
  • 36
    • 2642656596 scopus 로고
    • The refined crystal structure of dimeric phospholipase A2 at 2.5 Å. Access to a shielded catalytic center
    • Brunie, S., Bolin, J., Gerwith, D., Sigler, P.B. The refined crystal structure of dimeric phospholipase A2 at 2.5 Å. Access to a shielded catalytic center J. Biol. Chem. 249: 3827-3835, 1985.
    • (1985) J. Biol. Chem. , vol.249 , pp. 3827-3835
    • Brunie, S.1    Bolin, J.2    Gerwith, D.3    Sigler, P.B.4
  • 37
    • 0026206788 scopus 로고
    • Sparse matrix sampling: A screening method for crystallization of proteins
    • Jancarik, J., Kim, S.H. Sparse matrix sampling: A screening method for crystallization of proteins. J. Appl. Crystallogr. 24:409-411, 1991.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 409-411
    • Jancarik, J.1    Kim, S.H.2
  • 39
    • 0001008852 scopus 로고
    • PROCESS: A program for indexing and processing R-AXIS II Imaging plate data
    • Higashi, T.J. PROCESS: A program for indexing and processing R-AXIS II Imaging plate data. J. Appl. Cryst. 23:253-257, 1990.
    • (1990) J. Appl. Cryst. , vol.23 , pp. 253-257
    • Higashi, T.J.1
  • 40
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza, J. AMoRe: An automated package for molecular replacement. Acta. Cryst. A50:157-163, 1994.
    • (1994) Acta. Cryst. , vol.A50 , pp. 157-163
    • Navaza, J.1
  • 41
    • 0003769049 scopus 로고
    • New Haven, CT: Yale Uninversity Press
    • Brünger, A. T.X-PLOR V3.0 manual. New Haven, CT: Yale Uninversity Press, 1992.
    • (1992) T.X-PLOR V3.0 Manual
    • Brünger, A.1
  • 42
    • 84889120137 scopus 로고
    • Improved methods for building 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. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta. Cryst. A47:110-119, 1991.
    • (1991) Acta. Cryst. , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 43
    • 0025398721 scopus 로고
    • WHATIF: A molecular modelling and drug design programm
    • Vriend, G. WHATIF: A molecular modelling and drug design programm. J. Mol. Graph. 8:52-55, 1990.
    • (1990) J. Mol. Graph. , vol.8 , pp. 52-55
    • Vriend, G.1
  • 46
    • 0015820465 scopus 로고
    • Synthesis and characterization of two fluorescent sulfhydryl reagents
    • Hudson, E.N. Weber, G. Synthesis and characterization of two fluorescent sulfhydryl reagents. Biochemistry 12:4154-4161, 1973.
    • (1973) Biochemistry , vol.12 , pp. 4154-4161
    • Hudson, E.N.1    Weber, G.2
  • 48
    • 0015230409 scopus 로고
    • Solute perturbation of protein fluorescence. the quenching of the tryptophyl fluorescence of model compounds and of lysozyme by iodide ion
    • Lehrer, S.S. Solute perturbation of protein fluorescence. The quenching of the tryptophyl fluorescence of model compounds and of lysozyme by iodide ion. Biochemistry 10:3254-3263, 1971.
    • (1971) Biochemistry , vol.10 , pp. 3254-3263
    • Lehrer, S.S.1
  • 49
    • 0021112292 scopus 로고
    • Structure of porcine PLA2 at 2.6 Angstrom resolution and comparison with bovine PLA2
    • Dijkstra, B.W., Renetseder, R., Kalk, K.H., Hol, W.G.J., Drenth, J. Structure of porcine PLA2 at 2.6 Angstrom resolution and comparison with bovine PLA2. J. Mol. Biol. 168:163-178, 1983.
    • (1983) J. Mol. Biol. , vol.168 , pp. 163-178
    • Dijkstra, B.W.1    Renetseder, R.2    Kalk, K.H.3    Hol, W.G.J.4    Drenth, J.5
  • 50
    • 0030201175 scopus 로고    scopus 로고
    • Phospholipases A2 - A structural review
    • Arni, R.K., Ward, R.J. Phospholipases A2 - A structural review. Toxicon 34:827-841, 1996.
    • (1996) Toxicon , vol.34 , pp. 827-841
    • Arni, R.K.1    Ward, R.J.2
  • 52
    • 0028034445 scopus 로고
    • Neutralizing interaction between heparin and myotoxin II, a Lys49 phospholipase A2 from Bothrops asper snake venom. Identification of a heparin-binding and cytolytic toxin region by the use of synthetic peptides and molecular modelling
    • Lomonte, B., Moreno, E., Tarkowski, A., Hanson, L.A., Maccarama, M. Neutralizing interaction between heparin and myotoxin II, a Lys49 phospholipase A2 from Bothrops asper snake venom. Identification of a heparin-binding and cytolytic toxin region by the use of synthetic peptides and molecular modelling. J. Biol. Chem. 269:29867-29873, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29867-29873
    • Lomonte, B.1    Moreno, E.2    Tarkowski, A.3    Hanson, L.A.4    Maccarama, M.5
  • 54
    • 0023046984 scopus 로고
    • Kinetics of interfacial catalysis by phospholipase A2 in intravesicle scooting mode, and heterofusion of anionic and zwitterionic vesicles
    • Jain, M.K., Rogers, J., Jahagirdar, D.V., Maracek, J.F., Ramirez, F. Kinetics of interfacial catalysis by phospholipase A2 in intravesicle scooting mode, and heterofusion of anionic and zwitterionic vesicles. Biochem. Biophys. Acta 860:435-447, 1986.
    • (1986) Biochem. Biophys. Acta , vol.860 , pp. 435-447
    • Jain, M.K.1    Rogers, J.2    Jahagirdar, D.V.3    Maracek, J.F.4    Ramirez, F.5
  • 55
    • 0026597444 scopus 로고
    • The free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger, A.T. The free R value: A novel statistical quantity for assessing the accuracy of crystal structures. Nature 355:472-474, 1992.
    • (1992) Nature , vol.355 , pp. 472-474
    • Brünger, A.T.1
  • 57
    • 0024246956 scopus 로고
    • Surface, subunit interfaces and interior of oligomeric proteins
    • Janin, J., Miller, S., Chothia, C. Surface, subunit interfaces and interior of oligomeric proteins. J. Mol. Biol. 204:155-164, 1988.
    • (1988) J. Mol. Biol. , vol.204 , pp. 155-164
    • Janin, J.1    Miller, S.2    Chothia, C.3


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