Crystallization and preliminary crystallographic analysis of SMase I, a sphingomyelinase from Loxosceles laeta spider venom

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dc.contributor.authorZela, S. P.
dc.contributor.authorPedrosa, MFF
dc.contributor.authorMurakami, M. T.
dc.contributor.authorde Andrade, S. A.
dc.contributor.authorArni, R. K.
dc.contributor.authorTambourgi, D. V.
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionInstituto Butantan
dc.date.accessioned2014-05-20T14:02:25Z
dc.date.available2014-05-20T14:02:25Z
dc.date.issued2004-06-01
dc.description.abstractSMase I, a 32 kDa sphingomyelinase found in Loxosceles laeta venom, is responsible for the major pathological effects of spider envenomation. This toxin has been cloned and functionally expressed as a fusion protein containing a 6 x His tag at its N-terminus to yield a 33 kDa protein [Fernandes-Pedrosa et al. (2002), Biochem. Biophys. Res. Commun. 298, 638 - 645]. The recombinant protein possesses all the biological properties ascribed to the whole L. laeta venom, including dermonecrotic and complement-dependent haemolytic activities. Dynamic light-scattering experiments conducted at 291 K demonstrate that the sample possesses a monomodal distribution, with a hydrodynamic radius of 3.57 nm. L. laeta SMase I was crystallized by the hanging-drop vapour-diffusion technique using the sparse-matrix method. Single crystals were obtained using a buffer solution consisting of 0.08 M HEPES and 0.9 M trisodium citrate, which was titrated to pH 7.5 using 0.25 M sodium hydroxide. Complete three-dimensional diffraction data were collected to 1.8 Angstrom at the Laboratorio Nacional de Luz Sincrotron (LNLS, Campinas, Brazil). The crystals belong to the hexagonal system ( space group P6(1) or P6(5)), with unit-cell parameters a = b = 140.6, c = 113.6 Angstrom. A search for heavy-atom derivatives has been initiated and elucidation of the crystal structure is currently in progress.en
dc.description.affiliationUNESP, IBILCE, Dept Phys, BR-15054000 Sao Jose do Rio Preto, SP, Brazil
dc.description.affiliationInstituto Butantan, Immunochem Lab, BR-05503900 São Paulo, Brazil
dc.description.affiliationUnespUNESP, IBILCE, Dept Phys, BR-15054000 Sao Jose do Rio Preto, SP, Brazil
dc.format.extent1112-1114
dc.identifierhttp://dx.doi.org/10.1107/S090744490400678X
dc.identifier.citationActa Crystallographica Section D-biological Crystallography. Copenhagen: Blackwell Munksgaard, v. 60, p. 1112-1114, 2004.
dc.identifier.doi10.1107/S090744490400678X
dc.identifier.issn0907-4449
dc.identifier.lattes9162508978945887
dc.identifier.orcid0000-0003-2460-1145
dc.identifier.urihttp://hdl.handle.net/11449/22006
dc.identifier.wosWOS:000221572600016
dc.language.isoeng
dc.publisherBlackwell Munksgaard
dc.relation.ispartofActa Crystallographica Section D: Biological Crystallography
dc.rights.accessRightsAcesso restrito
dc.sourceWeb of Science
dc.titleCrystallization and preliminary crystallographic analysis of SMase I, a sphingomyelinase from Loxosceles laeta spider venomen
dc.typeArtigo
dcterms.licensehttp://olabout.wiley.com/WileyCDA/Section/id-406071.html
dcterms.rightsHolderBlackwell Munksgaard
unesp.author.lattes9162508978945887[5]
unesp.author.orcid0000-0003-2460-1145[5]
unesp.campusUniversidade Estadual Paulista (Unesp), Instituto de Biociências Letras e Ciências Exatas, São José do Rio Pretopt

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