1H-NMR-derived secondary structure and the overall fold of the potent anti-mammal and anti-insect toxin III from the scorpion Leiurus quinquestriatus quinquestriatus

European Journal of Biochemistry

Volumn 236, Issue 2, 1996, Pages 395-404

  Landon, Céline ^a   Cornet, Bruno ^a   Bonmatin, Jean Marc ^a   Kopeyan, Charles ^b   Rochat, Hervé ^b   Vovelle, Françoise ^a,c   Ptak, Marius ^a,c  

^a CENTRE DE BIOPHYSIQUE MOLÉCULAIRE   (France)

^b CNRS   (France)

^c UNIVERSITÉ D'ORLÉANS   (France)

Author keywords

defensin; NMR; scorpion; structure; toxin

Indexed keywords

SCORPION VENOM; TOXIN; DISULFIDE; LEIURUTOXIN III; NEUROTOXIN; PEPTIDE;

ARTICLE; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; NUCLEAR OVERHAUSER EFFECT; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STRUCTURE; SCORPION; AMINO ACID SEQUENCE; CHEMICAL STRUCTURE; CHEMISTRY; COMPARATIVE STUDY; COMPUTER SIMULATION; MOLECULAR GENETICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY;

HEXAPODA; INSECTA; LEIURUS; LEIURUS QUINQUESTRIATUS QUINQUESTRIATUS; MAMMALIA; SCORPIONES;

AMINO ACID SEQUENCE; COMPUTER SIMULATION; DISULFIDES; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NEUROTOXINS; PEPTIDES; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SCORPION VENOMS; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 0029670286     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1996.00395.x     Document Type: Article

References (59)

1. 5A, FEBS Lett. 165, 57-62.
2. Bartels, C., Xia, T.-E., Billeter, M., Güntert, P. & Wüthrich, K. (1995) The program XEASY for computer-supported NMR spectral analysis of biological macromolecules, J. Biomol. NMR 5, 1-10.
3. Bax, A. & Davis, D. G. (1985) MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy, J. Magn. Reson. 65, 355-360.
4. 1H-NMR, Eur. J. Biochem. 196, 19-28.
5. Braun, W. & Go, N. (1985) Calculation of protein conformations by proton-proton distance constraints, J. Mol. Biol. 186, 611-169.
6. Brooks, B., Brucoli, R., Olafson, B. O., States, D., Swaminathan, S. & Karplus, M. (1983) CHARMM: a program for macromolecular energy, minimization, and dynamics calculations. J. Comput. Chem. 4, 187-217.
7. 1H NMR spectra in proteins, J. Magn. Reson. 77, 166-169.
8. 1H-NMR: a structural motif common to toxic arthropod proteins, Biochemistry 32, 715-724.
9. Brünger, A. T., Clore, G. M., Gronenborn, A. M. & Karplus, M. (1986) Three-dimensional structure of proteins determined by molecular dynamics with interproton distance restraints: application to crambin, Proc. Natl Acad. Sci. USA 83, 3801-3805.
10. Catterall, W. A. (1986) Molecular properties of voltage-sensitive sodium channels. Annu. Rev. Biochem. 55, 953-985.
11. Cornet, B., Bonmatin, J.-M., Hetru, C., Hoffmann, J. A., Ptak, M. & Vovelle, F. (1995) Refined three-dimensional solution structure of insect defensin A, Structure 3, 435-448.
12. Couraud, F., Jover, E., Dubois, J. M. & Rochat, H. (1982) Two types of scorpion toxin receptor sites, one related to the activation, the other to the inactivation of the action potential sodium channel, Toxicon 20, 9-16.
13. Darbon, H., Zlotkin, E., Kopeyan, C. Van Rietschoten, J. & Rochat, H. (1982) Covalent structure of the insect toxin of the North African scorpion Androctonus australis Hector. Int. J. Pept. Protein Res. 20, 320-330.
14. 1H nuclear magnetic resonance study of AaH IT, an anti-insect toxin from the scorpion Androctonus australis Hector. Sequential resonance assignments and folding of the polypeptide chain, Biochemistry 30, 1836-1845.
15. De Lima, M. E., Martin, M. F., Diniz, C. R. & Rochat, H. (1986) Tityus serrulatus toxin VII bears pharmacological properties of both β-toxin and insect toxin from scorpion venoms, Biochem. Biophys. Res. Commun. 139, 296-302.
16. Eccles, C., Güntert, P., Billeter, M. & Wüthrich, K. (1991) Efficient analysis of protein 2D NMR spectra using the software package EASY, J. Biomol. NMR 1, 111-130.
17. Efimov, A. V. (1993) Standard structures in proteins, Prog. Biophys. Mol. Biol. 60, 201-239.
18. Fernández, I., Romi, R., Szendeffy, S., Martin-Eauclaire, M. F., Rochat, H., Van Rietschoten, J., Pons, M. & Giralt, E. (1994) Kaliotoxin (1-37) shows structural differences with related potassium channel blockers, Biochemistry 33, 14 256-14 263.
19. Fontecilla-Camps, J. C. Habersetzer-Rochat, C. & Rochat, H. (1988) Orthorhombic crystals and three-dimensional structure of the potent toxin II from the scorpion Andmctonus australis Hector, Proc. Natl Acad. Sci. USA 85, 7443-7447.
20. Fontecilla-Camps, J. C. (1989) Three-dimensional model of the insect-directed scorpion toxin from Andmctonus australis Hector and its implication for the evolution of scorpion toxins in general. J. Mol. Evol. 29, 63-67.
21. Gregoire, J. & Rochat, H. (1983) Covalent structure of toxins I and II from the scorpion Buthus occitanus tunetanus, Toxicon 21, 153-162.
22. 1H spin system identification in macromolecules, J. Am. Chem. Soc. 110, 7870-7872.
23. Güntert, P., Braun, W. & Wüthrich, K. (1991) Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA, J. Mol. Biol. 217, 517-530.
24. Housset, D., Habersetzer-Rochat, C., Astier, J.-P. & Fontecilla-Camps, J. C. (1994) Crystal structure of toxin II from the scorpion Androctonus australis Hector refined at 1.3 Å resolution. J. Mol. Biol. 238, 88-103.
25. Jablonsky, M. J., Watt, D. D. & Krishna, N. R. (1995) Solution structure of an Old World-like neurotoxin from the venom of the New World scorpion Centruroides sculpturatus Ewing. J. Mol. Biol. 248, 449-458.
26. Jeener, J., Meier, B. H., Bachmann, P. & Ernst, R. R. (1979) Investigation of exchange processes by two-dimensional NMR spectroscopy, J. Chem. Phys. 71, 4546-4553.
27. 1H nuclear magnetic resonance spectroscopy. Biochemistry 31, 8151-8159.
28. 15N triple-resonance nuclear magnetic resonance spectroscopy. Biochemistry 33, 15061-15070.
29. Kharrat, R., Darbon, H., Granier, C. & Rochat, H. (1990) Structure-activity relationships of scorpion α-neurotoxins: contribution of arginine residues. Toxicon 28, 509-523.
30. Kopeyan, C., Martinez, G., Lissitzky, S., Miranda, F. & Rochat, H. (1974) Disulfide bonds of toxin II of the scorpion Androctonus australis Hector, Eur. J. Biochem. 47, 483-489.
31. Kopeyan, C., Mansuelle, P., Sampieri, F., Brando, T., Bahraoui, E. M., Rochat, H. & Granier, C. (1990) Primary structure of scorpion anti-insect toxins isolated from the venom of Leiurus quinquestriatus quinquestriatus, FEBS Lett. 261, 423-426.
32. Kopeyan, C., Mansuelle, P., Martin-Eauclaire, M-F., Rochat, H. & Miranda, F. (1993) Characterization of toxin III of the scorpion Leiurus quinquestriatus quinquestriatus: a new type of alpha-toxin highly toxic both to mammals and insects. Natural Toxins 1, 308-312.
33. Kraulis, P. J. (1991) MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950.
34. Krishna, N. R., Nettesheim, D. G., Klevit, R. E., Drobny, G., Watt, D. D. & Bugg, C. E. (1989) Proton nuclear magnetic resonance characterization of the aromatic residues in the variant-3 neurotoxin from Centruroides sculpturatus Ewing, Biochemistry 28, 1556-1562.
35. Lebreton, F., Delepierre, M., Ramírez, A. N., Balderas, C. & Possani, L. D. (1994) Primary and NMR three-dimensional structure determination of a novel crustacean toxin from the venom of the scorpion Centruroides limpidus limpidus Karsch, Biochemistry 33, 11 135-11 149.
36. Lee, W., Moore, C. H., Watt, D. D. & Krishna, N. R. (1994a) Solution structure of the variant-3 neurotoxin from Centruroides sculpturatus Ewing, Eur. J. Biochem. 218, 89-95.
37. Lee, W., Jablonsky, M. J., Watt, D. D. & Krishna, N. R. (1994b) Proton nuclear magnetic resonance and distance geometry/simulated annealing studies on the variant-1 neurotoxin from the New World scorpion Centruroides sculpturatus Ewing, Biochemistry 33, 2468-2475.
38. Lippens, G., Najib, J., Wodak, S. J. & Tartar, A. (1995) NMR sequential assignments and solution structure of chlorotoxin, a small scorpion toxin that blocks chloride channels, Biochemistry 34, 13-21.
39. Loret, E. P., Sampieri, F., Roussel, A., Granier, C. & Rochat, H. (1990) Conformational flexibility of a scorpion toxin active on mammals and insects: a circular dichroism study, Proteins 8, 164-172.
40. Loret, E. P., Martin-Eauclaire, M.-F., Mansuelle, P., Sampieri, F., Granier, C. & Rochat, H. (1991) An anti-insect toxin purified from the scorpion Androctonus australis Hector also acts on the α- and β-sites of the mammalian sodium channel: sequence and circular dichroism study, Biochemistry 30, 633-640.
41. 1H spin-spin coupling constants in proteins, Biochem. Biophys. Res. Commun. 113, 967-974.
42. Martin-Eauclaire, M. F. & Couraud, F. (1995) Scorpion Neurotoxins: Effects and Mechanisms, in Handbook of neurotoxicology (Chang, L. W. & Dyer, R. S., eds) pp. 683-716, Marcel Dekker Inc., New York.
43. 1H chemical shifts obtained as a function of temperature and trifluoro-ethanol concentration for the peptide series GGXGG, J. Biomol. NMR 5, 14-24.
44. 2, a scorpion toxin analog with high affinity for the apamin-sensitive potassium channel, Biochemistry 32, 11 969-11 976.
45. Mikou, A., La Plante, S. R., Guittet, E., Lallemand, J.-Y., Martin-Eauclaire, M. F. & Rochat, H. (1992) Toxin III of the scorpion Androctonus australis Hector: proton nuclear magnetic resonance assignments and secondary structure, J. Biomol. NMR 2, 57-70.
46. Miranda, P., Kopeyan, C., Rochat, H., Rochat, C. & Lissitzky, S. (1970) Purification of animal neurotoxins, Eur. J. Biochem. 16, 514-523.
47. Nilges, M., Clore, G. M. & Gronenborn, A. M. (1988) Determination of three-dimensional structures of proteins from interproton distance data by dynamical simulated annealing from a random array of atoms, FEBS Lett. 239, 129-136.
48. Otting, G. (1990) Zero-quantum suppression in NOESY and experiments with a z filter, J. Magn. Reson. 86, 496-508.
49. Pagel, M. D. & Wemmer, D. E. (1994) Solution structure of a core peptide derived from scyllatoxin, Proteins 18, 205-215.
50. 1H-NMR spectroscopy, Biophys. Chem. 31, 121-131.
51. Piantini, U., Sørensen, O. W. & Ernst, R. R. (1982) Multiple quantum filters for elucidating NMR coupling networks, J. Am. Chem. Soc. 104, 6800-6801.
52. Plateau, P. & Guéron, M. (1982) Exchangeable proton NMR without base-line distortion, using new strong-pulse sequences, J. Am. Chem. Soc. 104, 7310-7311.
53. Ranee, M., Bodenhausen, G., Wagner, G., Wüthrich, K. & Ernst, R. R. (1985) A systematic approach to the suppression of J cross peaks in 2D exchange and 2D NOE spectroscopy, J. Magn. Reson. 62, 497-510.
54. Shaka, A. J. & Freeman, R. (1983) Simplification of NMR spectra by filtration through multiple-quantum coherence, J. Magn. Reson. 51, 169-173.
55. Sibanda, B. L., Blundell, T. L. & Thornton, J. M. (1989) Conformation of β-hairpins in protein structures. A systematic classification with applications to modelling by homology, electron density fitting and protein engineering, J. Mol. Biol. 206, 759-777.
56. States, D. J., Haberkorn, R. A. & Rubens, D. J. (1982) A two-dimensional nuclear overhauser experiment with pure absorption phase in four quadrants, J. Magn. Reson. 48, 286-292.
57. Szyperski, T., Güntert, P., Otting, G. & Wüthrich, K. (1992) Determination of scalar coupling constants by inverse fourier transformation of in-phase multiplets, J. Magn. Reson. 99, 552-560.
58. Wüthrich, K. (1986) NMR of proteins and nucleic acids, Wiley Interscience, New York.
59. Zhao, B., Carson, M., Ealick, S. E. & Bugg, C. E. (1992) Structure of scorpion toxin variant-3 at 1.2 Å resolution, J. Mol. Biol. 227, 239-252.