Fernandes, Carlos A. H. [UNESP]Gartuzo, Elaine C. G. [UNESP]Pagotto, Ivan [UNESP]Comparetti, Edson J. [UNESP]Huancahuire-Vega, SalomonPonce-Soto, Luis AlbertoCosta, Tassia R.Marangoni, SergioSoares, Andreimar M.Fontes, Marcos R. M. [UNESP]2014-05-202014-05-202012-08-01Acta Crystallographica Section F-structural Biology and Crystallization Communications. Hoboken: Wiley-blackwell, v. 68, p. 935-938, 2012.1744-3091http://hdl.handle.net/11449/17711Two 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 A2.935-938engphospholipases A2Bothrops brazilibraziliantoxin-IIbraziliantoxin-IIIMT-IIArtigo10.1107/S1744309112026073WOS:000307217700019Acesso restritoWOS000307217700019.pdf