Insights into metal ion binding in phospholipases A(2): ultra high-resolution crystal structures of an acidic phospholipase A(2) in the Ca2+ free and bound states

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dc.contributor.authorMurakami, M. T.
dc.contributor.authorGabdoulkhakov, A.
dc.contributor.authorGenov, N.
dc.contributor.authorCintra, A. C. O.
dc.contributor.authorBetzel, C.
dc.contributor.authorArni, R. K.
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionRussian Acad Sci
dc.contributor.institutionBulgarian Acad Sci
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.contributor.institutionInst Med Biochem & Mol Biol
dc.contributor.institutionInstituto Butantan
dc.date.accessioned2014-05-20T14:02:18Z
dc.date.available2014-05-20T14:02:18Z
dc.date.issued2006-05-01
dc.description.abstractThe electrophile Ca2+ is an essential multifunctional co-factor in the phospholipase A(2) mediated hydrolysis of phospholipids. Crystal structures of an acidic phospholipase A(2) from the venom of Bothrops jararacussu have been determined both in the Ca2+ free and bound states at 0.97 and 1.60 angstrom resolutions, respectively. In the Ca2+ bound state, the Ca2+ ion is penta-coordinated by a distorted pyramidal cage of oxygen and nitrogen atoms that is significantly different to that observed in structures of other Group I/II phospholipases A(2). In the absence of Ca2+, a water molecule occupies the position of the Ca2+ ion and the side chain of Asp49 and the calcium-binding loop adopts a different conformation. (c) 2005 Elsevier SAS. All rights reserved.en
dc.description.affiliationUNESP, IBILCE, Dept Phys, BR-15054000 Sao Jose do Rio Preto, SP, Brazil
dc.description.affiliationRussian Acad Sci, Inst Prot Res, Pushchino 142290, Moscow Region, Russia
dc.description.affiliationBulgarian Acad Sci, Inst Organ Chem, BU-1113 Sofia, Bulgaria
dc.description.affiliationUSP, Dept Biochem, BR-14040902 Ribeirao Preto, Brazil
dc.description.affiliationInst Med Biochem & Mol Biol, D-22603 Hamburg, Germany
dc.description.affiliationInstituto Butantan, Ctr Appl Toxinol, BR-05503900 São Paulo, Brazil
dc.description.affiliationUnespUNESP, IBILCE, Dept Phys, BR-15054000 Sao Jose do Rio Preto, SP, Brazil
dc.format.extent543-549
dc.identifierhttp://dx.doi.org/10.1016/j.biochi.2005.10.014
dc.identifier.citationBiochimie. Paris: Elsevier France-editions Scientifiques Medicales Elsevier, v. 88, n. 5, p. 543-549, 2006.
dc.identifier.doi10.1016/j.biochi.2005.10.014
dc.identifier.issn0300-9084
dc.identifier.lattes9162508978945887
dc.identifier.orcid0000-0003-2460-1145
dc.identifier.urihttp://hdl.handle.net/11449/21958
dc.identifier.wosWOS:000239270500015
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofBiochimie
dc.relation.ispartofjcr3.188
dc.relation.ispartofsjr1,554
dc.rights.accessRightsAcesso restrito
dc.sourceWeb of Science
dc.subjectsnake venompt
dc.subjectphospholipase A(2)pt
dc.subjectCa2+ coordinationpt
dc.subjectanticoagulant activitypt
dc.subjectX-ray analysispt
dc.titleInsights into metal ion binding in phospholipases A(2): ultra high-resolution crystal structures of an acidic phospholipase A(2) in the Ca2+ free and bound statesen
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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