Structure of acidic phospholipase A2 for the venom of Agkistrodon halys blomhoffii at 2.8Åresolution

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Abstract

The crystal structure of acidic phospholipase A2 from the venom of Agkistrodon halys blomhoffii has been determined by molecular replacement methods based on the known structure of Crotalus atrox PLA2, a same group II enzyme. The overall structures, except the calcium-binding regions, are very similar to each other. A calcium ion is pentagonally ligated to two car☐ylate oxygen atoms of Asp-49 and each carbonyl oxygen atoms of Tyr-28 ,Gly-30 and Ala-31. A reason why the former enzyme functions as monomeric form, while the latter one does as dimer, could be presumed by the structural comparison of these calcium-binding regions. Although Gly-32 is usually participated as a ligand in the coordination with calcium ion in group I PLA2, it is characteristically replaced to Ala-31 in the present structure, and thus the coordination geometry of calcium ion is rather different from the usually observed one.

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    AY764138 and AY764139). While expressed at low level, single E6W30-PLA2 has been identified in D. acutus (Tsai, 1997) and single E6A30-PLA2 has been identified in the venom of Chinese G. shedaoensis (Jin et al., 2004), Japanese G. blomhoffii (Tomoo et al., 1992), and Costa Rican Bothriechis schlegelii venom (Chen et al., 2004). Among the pitviper acidic PLA2s, the W30 and the A30 substitutions are rather common and possibly original (Fig. 1A and B), followed by the K30 and S30 substitutions (Tsai et al., 2004a, 2004b).

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