Preliminary X-ray crystallographic studies of a tetrameric phospholipase A2 formed by two isoforms of crotoxin B from Crotalus durissus terrificus venom

• Published in: Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2007-12, Vol.63 (12), p.1067-1069
• Main Authors: Marchi-Salvador, D. P., Corrêa, L. C., Salvador, G. H. M., Magro, A. J., Oliveira, C. Z., Iulek, J., Soares, A. M., Fontes, M. R. M.
• Format: Article
• Language: English
• Subjects: Animals; Crotalus - genetics; Crotalus - metabolism; Crotoxin - chemistry; Crotoxin - genetics; Crotoxin - metabolism; crotoxin B; Crystallization; Crystallization Communications; Isoenzymes - chemistry; Isoenzymes - metabolism; Models, Molecular; phospholipase A2; Phospholipases A2 - chemistry; Phospholipases A2 - genetics; Phospholipases A2 - metabolism; Protein Binding; Protein Structure, Quaternary; snake venoms; Snake Venoms - chemistry; Snake Venoms - genetics; Snake Venoms - metabolism; X-Ray Diffraction
• ISSN: 1744-3091; 1744-3091
• DOI: 10.1107/S1744309107058563

Crotoxin B is a basic phospholipase A2 found in the venom of Crotalus durissus terrificus and is one of the subunits that constitute crotoxin. This heterodimeric toxin, which is the main component of C. d. terrificus venom, is completed by an acidic, nontoxic and non‐enzymatic component (crotoxin A) and is involved in important envenomation effects, such as neurological disorders, myotoxicity and renal failure. Although crotoxin was first crystallized in 1938, no crystal structure is currently available for crotoxin, crotoxin A or crotoxin B. In this work, the crystallization, X‐ray diffraction data collection to 2.28 Å resolution and molecular‐replacement solution of a novel tetrameric complex formed by two dimers of crotoxin B isoforms (CB1 and CB2) is presented.