Structure of a Lys49 phospholipase A(2) homologue isolated from the venom of Bothrops nummifer (jumping viper)
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1999-02-01
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Elsevier B.V.
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Lys49-Phospholipase A(2) (Lys49-PLA(2)) homologues damage membranes by a Ca2+-independent mechanism which does not involve catalytic activity, We have solved the structure of myotoxin-I, a Lys49-PLA(2) homologue isolated from the venom of Bothrops nummifer (jumping viper) at 2.4 Angstrom resolution using molecular replacement techniques. The final model has been refined to a final R-factor of 18.4% (R-free = 23.2%), and shows excellent geometry, the myotoxin-I from Bothrops nummifer is dimeric in the crystalline state as has been observed for other Lys49-PLA(2) homologues. In addition, a continuous electron density in the active site and substrate binding channel could be successfully modeled as a fatty-acid molecule. (C) 1999 Elsevier B.V. Ltd, All rights reserved.
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Toxicon. Oxford: Pergamon-Elsevier B.V., v. 37, n. 2, p. 371-384, 1999.
