Preliminary cryocrystallography analysis of an eumenine mastoparan toxin isolated from the venom of the wasp Anterhynchium flavomarginatum micado
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Data
2001-02-09
Autores
Delatorre, P.
Olivieri, JR
Neto, JR
Lorenzi, CCB
Canduri, F.
Fadel, V
Konno, K.
Palma, Mario Sergio [UNESP]
Yamane, T.
de Azevedo, W. F.
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Editor
Elsevier B.V.
Resumo
Mastoparans are tetradecapeptides found to be the major component of vespid venoms. These peptides present a wide spectrum of biological activities, such as mast cell degranulation, hemolytic activity and also reveals antimicrobial activity. A mastoparan toxin isolated from the venom of Anterhynchium flavomarginatum micado has been crystallized. At room temperature these crystals diffracted to 2.8 Angstrom resolution. However, upon cooling to cryogenic temperature around 85 K, the original resolution limit could be improved to 2.0 Angstrom. Crystals were determined to belong to the space group P3(1) (P3(2)). This is the first mastoparan to be crystallized and it will provide further insights in the conformational significance of mastoparan toxins, with respect to their potency and activity in G protein regulation. (C) 3001 Elsevier B.V. B.V. All rights reserved.
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mastoparan, cryocrystallography, synchrotron, wasp
Como citar
Biochimica Et Biophysica Acta-protein Structure and Molecular Enzymology. Amsterdam: Elsevier B.V., v. 1545, n. 1-2, p. 372-376, 2001.