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Type: | Artigo |
Title: | Crystallization and preliminary X-ray diffraction analysis of three myotoxic phospholipases A2 from Bothrops brazili venom |
Author: | Fernandes, Carlos A. H. Gartuzo, Elaine C. G. Pagotto, Ivan Comparetti, Edson J. Huancahuire-Vega, Salomon Ponce-Soto, Luis Alberto Costa, Tassia R. Marangoni, Sergio Soares, Andreimar M. Fontes, Marcos R. M. |
Abstract: | Two myotoxic and noncatalytic Lys49-phospholipases A2 (braziliantoxin-II and MT-II) and a myotoxic and catalytic phospholipase A2 (braziliantoxin-III) from the venom of the Amazonian snake Bothrops brazili were crystallized. The crystals diffracted to resolutions in the range 2.562.05 angstrom and belonged to space groups P3121 (braziliantoxin-II), P6522 (braziliantoxin-III) and P21 (MT-II). The structures were solved by molecular-replacement techniques. Both of the Lys49-phospholipases A2 (braziliantoxin-II and MT-II) contained a dimer in the asymmetric unit, while the Asp49-phospholipase A2 braziliantoxin-III contained a monomer in its asymmetric unit. Analysis of the quaternary assemblies of the braziliantoxin-II and MT-II structures using the PISA program indicated that both models have a dimeric conformation in solution. The same analysis of the braziliantoxin-III structure indicated that this protein does not dimerize in solution and probably acts as a monomer in vivo, similar to other snake-venom Asp49-phospholipases A2 |
Subject: | Fosfolipases A2 |
Country: | Estados Unidos |
Editor: | Wiley-Blackwell |
Rights: | Aberto |
Identifier DOI: | 10.1107/S1744309112026073 |
Address: | http://scripts.iucr.org/cgi-bin/paper?S1744309112026073 |
Date Issue: | 2012 |
Appears in Collections: | IB - Artigos e Outros Documentos |
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000307217700019.pdf | 357.8 kB | Adobe PDF | View/Open |
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