Isolation and preliminary crystallographic studies of two new phospholipases A2 from Vipera nikolskii venom.
Snake-venom phospholipases A2 (PLA2s) 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 PLA2 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 A2 activity and may possess neurotoxic activity. Based on the determined partial amino-acid sequences, the new proteins can be classified as basic Asp49 phospholipases A2. They were crystallized using the hanging-drop vapour-diffusion method and crystals of both proteins belong to space group R32, with similar unit-cell parameters: a = b = 76.29, c = 303.35 A for protein VN5-3 and a = b = 76.28, c = 304.39 A for protein VN4-3. Diffraction data sets to 3.0 and 2.2 A 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 PLA2s.
Gao
Wei
W
Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, People's Republic of China.
Starkov
Vladislav G
VG
Tsetlin
Victor I
VI
Utkin
Yuri N
YN
Lin
Zheng-jiong
ZJ
Bi
Ru-chang
RC
D000818:Animals; D018360:Crystallography, X-Ray; D006135:Gryllidae; D007527:Isoenzymes / Q000737:chemistry / Q000302:isolation & purification; D008970:Molecular Weight; D010741:Phospholipases A / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*; D054467:Phospholipases A2; D014757:Viper Venoms / Q000633:toxicity; D017819:Viperidae; D014961:X-Ray Diffraction
D007527:Isoenzymes; D014757:Viper Venoms; D010741:Phospholipases A; D054467:Phospholipases A2