Abstract
Phospholipases A2 are components of Bothrops venoms responsible for disruption of cell membrane integrity via hydrolysis of its phospholipids. A class of PLA2-like proteins has been described which despite PLA2 activity on artificial substrate, due to a D49K mutation, is still highly myonecrotic. This work reports the X-ray structure determination of two Lys49-PLA2s from Bothrops neuwiedi pauloensis (BnSP-7 and BnSP-6) and, for the first time, the comparison of eight dimeric Lys49-PLA2s. This comparison reveals that there are not just two (“open” and “closed”) but at least six different conformations. The binding of fatty acid observed in three recent Lys49-PLA2 structures seems to be independent of their quaternary conformation. Cys29 polarization by Lys122 is not significant for BnSP-7 and BnSP-6 or other structures not bound by fatty acids. These structures may be in an “active” state when nothing is bound to them and the Lys122/Cys29 interactions are weak or absent.
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