Open AccessComplete amino‐acid sequence, crystallization and preliminary X‐ray diffraction studies of leucurolysin‐a, a nonhaemorrhagic metalloproteinase from Bothrops leucurus snake venom
Author(s) -
Ferreira Rodrigo Novaes,
Rates Breno,
Richardson Michael,
Guimarães Beatriz Gomes,
Sanchez Eládio Oswaldo Flores,
Pimenta Adriano Monteiro de Castro,
Nagem Ronaldo Alves Pinto
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109025767
Subject(s) - venom , snake venom , peptide sequence , biology , enzyme , metalloproteinase , biochemistry , bothrops jararaca , chemistry , microbiology and biotechnology , gene
Leucurolysin‐a (leuc‐a) is a class P‐I snake‐venom metalloproteinase isolated from the venom of the South American snake Bothrops leucurus (white‐tailed jararaca). The mature protein is composed of 202 amino‐acid residues in a single polypeptide chain. It contains a blocked N‐terminus and is not glycosylated. In vitro studies revealed that leuc‐a dissolves clots made either from purified fibrinogen or from whole blood. Unlike some other venom fibrinolytic metalloproteinases, leuc‐a has no haemorrhagic activity. Leuc‐a was sequenced and was crystallized using the hanging‐drop vapour‐diffusion technique. Crystals were obtained using PEG 6000 or PEG 1500. Diffraction data to 1.80 and 1.60 Å resolution were collected from two crystals (free enzyme and the endogenous ligand–protein complex, respectively). They both belonged to space group P 2 1 2 1 2 1 , with very similar unit‐cell parameters ( a = 44.0, b = 56.2, c = 76.3 Å for the free‐enzyme crystal).