Crystal structure of piratoxin-I: A calcium-independent, myotoxic phospholipase A(2)-homologue from Bothrops pirajai venom

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dc.contributor.authorDe Azevedo, W. F.
dc.contributor.authorWard, R. J.
dc.contributor.authorCanduri, F.
dc.contributor.authorSoares, A.
dc.contributor.authorGiglio, JR
dc.contributor.authorArni, R. K.
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.date.accessioned2014-05-20T14:02:22Z
dc.date.available2014-05-20T14:02:22Z
dc.date.issued1998-10-01
dc.description.abstractThe crystal structure of Piratoxin-I (PrTX-I) a Lys49 homologue isolated from the venom of Bothrops pirajai has been determined and refined at 2.8 Angstrom to a crystallographic residual of 19.7% (R-free = 29.7%). Amino-acid sequence differences between catalytically active phospholipases and PrTX-I in the putative Ca2+-binding loop, specifically the substitutions Tyr28-->Asn, Gly32-->Leu and Asp49-->Lys, result in an altered conformation of this loop, the analysis of the position of the E-amino group of Lys49 in the PrTX-I structure indicates that it fills the site normally occupied by the calcium ion in the catalytically active phospholipases, In contrast to the homologous monomeric Lys49 variant from Agkistrodon piscivorus piscivorus (App), PrTX-I is present as a dimer in the crystalline state, as observed in the structures of myotoxin II from Bothrops asper and Bothropstoxin I from Bothrops jararacussu. The two molecules in the asymmetric unit in the crystal structure of PrTX-I are related by a nearly perfect two-fold symmetry axis, yet the dimeric structure is radically different from the dimeric structure of the phospholipase from Crotalus atrox. In the C. atrox structure the dimer interface occludes the active sites, whereas in the PrTX-I structure they are exposed to solvent, (C) 1998 Elsevier B.V. Ltd. All rights reserved.en
dc.description.affiliationUNESP, IBILCE, Dept Phys, BR-15054000 Sao Jose do Rio Preto, SP, Brazil
dc.description.affiliationUSP, FMRP, Dept Biochem, BR-14049900 Ribeirao Preto, SP, Brazil
dc.description.affiliationUnespUNESP, IBILCE, Dept Phys, BR-15054000 Sao Jose do Rio Preto, SP, Brazil
dc.format.extent1395-1406
dc.identifierhttp://dx.doi.org/10.1016/S0041-0101(98)00017-8
dc.identifier.citationToxicon. Oxford: Pergamon-Elsevier B.V., v. 36, n. 10, p. 1395-1406, 1998.
dc.identifier.doi10.1016/S0041-0101(98)00017-8
dc.identifier.issn0041-0101
dc.identifier.lattes9162508978945887
dc.identifier.orcid0000-0003-2460-1145
dc.identifier.urihttp://hdl.handle.net/11449/21985
dc.identifier.wosWOS:000075263700008
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofToxicon
dc.relation.ispartofjcr2.352
dc.relation.ispartofsjr0,692
dc.rights.accessRightsAcesso restrito
dc.sourceWeb of Science
dc.titleCrystal structure of piratoxin-I: A calcium-independent, myotoxic phospholipase A(2)-homologue from Bothrops pirajai venomen
dc.typeArtigo
dcterms.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dcterms.rightsHolderElsevier B.V.
unesp.author.lattes9162508978945887[6]
unesp.author.orcid0000-0003-2460-1145[6]
unesp.campusUniversidade Estadual Paulista (Unesp), Instituto de Biociências Letras e Ciências Exatas, São José do Rio Pretopt

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