Crystallization and preliminary X-ray diffraction analysis of a class II phospholipase D from Loxosceles intermedia venom

• Main Author: Ullah, Anwar [UNESP]
• Publication Date: 2011
• Other Authors: de Giuseppe, Priscila Oliveira, Murakami, Mario Tyago, Trevisan-Silva, Dilza, Martins Wille, Ana Carolina, Chaves-Moreira, Daniele, Gremski, Luiza Helena, da Silveira, Rafael Bertoni, Sennf-Ribeiro, Andrea, Chaim, Olga Meiri, Veiga, Silvio Sanches, Arni, Raghuvir Krishnaswamy [UNESP]
• Format: Article
• Language: eng
• Source: Repositório Institucional da UNESP
• Download full: http://dx.doi.org/10.1107/S1744309110050931; http://hdl.handle.net/11449/22098

Phospholipases D are the major dermonecrotic component of Loxosceles venom and catalyze the hydrolysis of phospholipids, resulting in the formation of lipid mediators such as ceramide-1-phosphate and lysophosphatidic acid which can induce pathological and biological responses. Phospholipases D can be classified into two classes depending on their catalytic efficiency and the presence of an additional disulfide bridge. In this work, both wild-type and H12A-mutant forms of the class II phospholipase D from L. intermedia venom were crystallized. Wild-type and H12A-mutant crystals were grown under very similar conditions using PEG 200 as a precipitant and belonged to space group P12(1)1, with unit-cell parameters a = 50.1, b = 49.5, c = 56.5 angstrom, beta = 105.9 degrees. Wild-type and H12A-mutant crystals diffracted to maximum resolutions of 1.95 and 1.60 angstrom, respectively.