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Purification, crystallization and preliminary x-ray crystallographic analysis of a phospholipase A2 from Daboia russelli pulchella.

作者信息

Chandra V, Nagpal A, Srinivasan A, Singh T P

机构信息

Department of Biophysics, All India Institute of Medical Sciences, New Delhi 110029, India.

出版信息

Acta Crystallogr D Biol Crystallogr. 1999 Apr;55(Pt 4):925-6. doi: 10.1107/s090744499900058x.

DOI:10.1107/s090744499900058x
PMID:10089336
Abstract

Phospholipases are esterolytic enzymes which hydrolyze glycerophospholipids. The pharmacological efficiency of phospholipase A2 (PLA2) enzymes is reflected by their specificity towards a tissue or organ. The Russell's viper has been classified into two classes. Class 1 contains Viper russelli russelli, Viper russelli siamensis and Viper russelli formosensis, whereas class 2 contains Daboia russelli pulchella. The sequence identity between the PLA2s from these two classes is 47%. The novel PLA2 from Daboia russelli pulchella has been crystallized using the hanging-drop vapour-diffusion method with ammonium sulfate as precipitating agent. Crystals belong to the orthorhombic space group C2221 with unit-cell parameters a = 77.01, b = 92.29, c = 76.90 A and two molecules in the asymmetric unit. These crystals diffract to about 2. 49 A resolution using a rotating-anode source.

摘要

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