Crystallization and preliminary X-ray diffraction analysis of three myotoxic phospholipases A2 from Bothrops brazili venom
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Data
2012-08-01
Autores
Fernandes, Carlos A. H. [UNESP]
Gartuzo, Elaine C. G. [UNESP]
Pagotto, Ivan [UNESP]
Comparetti, Edson J. [UNESP]
Huancahuire-Vega, Salomon
Ponce-Soto, Luis Alberto
Costa, Tassia R.
Marangoni, Sergio
Soares, Andreimar M.
Fontes, Marcos R. M. [UNESP]
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Título de Volume
Editor
Wiley-Blackwell
Resumo
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.
Descrição
Palavras-chave
phospholipases A2, Bothrops brazili, braziliantoxin-II, braziliantoxin-III, MT-II
Como citar
Acta Crystallographica Section F-structural Biology and Crystallization Communications. Hoboken: Wiley-blackwell, v. 68, p. 935-938, 2012.