Open AccessIsolation and preliminary crystallographic studies of two new phospholipases A 2 from Vipera nikolskii venom
Author(s) -
Gao Wei,
Starkov Vladislav G.,
Tsetlin Victor I.,
Utkin Yuri N.,
Lin Zhengjiong,
Bi Ruchang
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309104033688
Subject(s) - venom , phospholipase , phospholipase a2 , crystallography , phospholipase a , chemistry , stereochemistry , biology , biochemistry , enzyme
Snake‐venom phospholipases A 2 (PLA 2 s) represent a good model for studies of structure–function relationships, mainly because of their small size and diverse pharmacological and toxicological activities. To obtain new members of the abundant PLA 2 family, the venom of the viper Vipera nikolskii was fractionated for the first time and two new proteins, VN5‐3 and VN4‐3, were isolated. Both proteins show phospholipase A 2 activity and may possess neurotoxic activity. Based on the determined partial amino‐acid sequences, the new proteins can be classified as basic Asp49 phospholipases A 2 . They were crystallized using the hanging‐drop vapour‐diffusion method and crystals of both proteins belong to space group R 32, with similar unit‐cell parameters: a = b = 76.29, c = 303.35 Å for protein VN5‐3 and a = b = 76.28, c = 304.39 Å for protein VN4‐3. Diffraction data sets to 3.0 and 2.2 Å resolution were collected and processed for the VN5‐3 and VN4‐3 crystals, respectively. Preliminary analysis indicates that there are two molecules in the asymmetric unit for both crystals. Further crystallographic studies will help in understanding the structural basis for the multiple functions of snake‐venom PLA 2 s.