Open AccessCrystallization and preliminary X‐ray crystallographic studies of a Lys49‐phospholipase A 2 homologue from Bothrops pirajai venom complexed with rosmarinic acid
Author(s) -
Dos Santos Juliana I.,
SantosFilho Norival A.,
Soares Andreimar M.,
Fontes Marcos R. M.
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110013709
Subject(s) - bothrops , venom , crystallography , crystallization , molecule , snake venom , phospholipase a2 , chemistry , stereochemistry , phospholipase a , biochemistry , enzyme , organic chemistry
PrTX‐I, a noncatalytic and myotoxic Lys49‐phospholipase A 2 from Bothrops pirajai venom, was crystallized in the presence of the inhibitor rosmarinic acid (RA). This is the active compound in the methanolic extract of Cordia verbenacea , a plant that is largely used in Brazilian folk medicine. The crystals diffracted X‐rays to 1.8 Å resolution and the structure was solved by molecular‐replacement techniques, showing electron density that corresponds to RA molecules at the entrance to the hydrophobic channel. The crystals belong to space group P 2 1 2 1 2 1 , indicating conformational changes in the structure after ligand binding: the crystals of all apo Lys49‐phospholipase A 2 structures belong to space group P 3 1 21, while the crystals of complexed structures belong to space groups P 2 1 or P 2 1 2 1 2 1 .