Complete amino-acid sequence, crystallization and preliminary X-ray diffraction studies of leucurolysin-a, a nonhaemorrhagic metalloproteinase from Bothrops leucurus snake venom.
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 A resolution were collected from two crystals (free enzyme and the endogenous ligand-protein complex, respectively). They both belonged to space group P2(1)2(1)2(1), with very similar unit-cell parameters (a = 44.0, b = 56.2, c = 76.3 A for the free-enzyme crystal).
Ferreira
Rodrigo Novaes
RN
Departamento de Bioquímica e Imunologia, Instituto de Ciências Biológicas, Universidade Federal de Minas Gerais, Avenida Antônio Carlos 6627, Belo Horizonte-MG, 31270-901, Brazil.
Rates
Breno
B
Richardson
Michael
M
Guimarães
Beatriz Gomes
BG
Sanchez
Eládio Oswaldo Flores
EO
Pimenta
Adriano Monteiro de Castro
AM
Nagem
Ronaldo Alves Pinto
RA
D000595:Amino Acid Sequence; D000818:Animals; D017837:Bothrops; D003435:Crotalid Venoms / Q000201:enzymology*; D018360:Crystallography, X-Ray; D045726:Metalloproteases / Q000737:chemistry*; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D053719:Tandem Mass Spectrometry
D003435:Crotalid Venoms; D045726:Metalloproteases