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. 2006 Aug 1;62(Pt 8):765-7.
doi: 10.1107/S1744309106025164. Epub 2006 Jul 24.

Preliminary X-ray crystallographic studies of BthTX-II, a myotoxic Asp49-phospholipase A2 with low catalytic activity from Bothrops jararacussu venom

L C Corrêa  1 , D P Marchi-Salvador, A C O Cintra, A M Soares, M R M Fontes
Affiliations

Preliminary X-ray crystallographic studies of BthTX-II, a myotoxic Asp49-phospholipase A2 with low catalytic activity from Bothrops jararacussu venom

L C Corrêa et al. Acta Crystallogr Sect F Struct Biol Cryst Commun. .

Abstract

For the first time, a complete X-ray diffraction data set has been collected from a myotoxic Asp49-phospholipase A2 (Asp49-PLA2) with low catalytic activity (BthTX-II from Bothrops jararacussu venom) and a molecular-replacement solution has been obtained with a dimer in the asymmetric unit. The quaternary structure of BthTX-II resembles the myotoxin Asp49-PLA2 PrTX-III (piratoxin III from B. pirajai venom) and all non-catalytic and myotoxic dimeric Lys49-PLA2s. In contrast, the oligomeric structure of BthTX-II is different from the highly catalytic and non-myotoxic BthA-I (acidic PLA2 from B. jararacussu). Thus, comparison between these structures should add insight into the catalytic and myotoxic activities of bothropic PLA2s.

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Figures

Figure 1
Figure 1
Crystals of BthTX-II from B. jararacussu venom
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