Structural insights into the catalytic mechanism of sphingomyelinases D and evolutionary relationship to glycerophosphodiester phosphodiesterases

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dc.contributor.authorMurakami, M. T.
dc.contributor.authorFernandes-Pedrosa, M. F.
dc.contributor.authorde Andrade, S. A.
dc.contributor.authorGabdoulkhakov, A.
dc.contributor.authorBetzel, C.
dc.contributor.authorTambourgi, D. V.
dc.contributor.authorArni, R. K.
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionInstituto Butantan
dc.contributor.institutionRAS
dc.contributor.institutionUniv Hamburg
dc.date.accessioned2014-05-20T14:02:23Z
dc.date.available2014-05-20T14:02:23Z
dc.date.issued2006-03-31
dc.description.abstractSpider venom sphingomyelinases D catalyze the hydrolysis of sphingomyelin via an Mg2+ ion-dependent acid-base catalytic mechanism which involves two histidines. In the crystal structure of the sulfate free enzyme determined at 1.85 angstrom resolution, the metal ion is tetrahedrally coordinated instead of the trigonal-bipyramidal coordination observed in the sulfate bound form. The observed hyperpolarized state of His47 requires a revision of the previously suggested catalytic mechanism. Molecular modeling indicates that the fundamental structural features important for catalysis are fully conserved in both classes of SMases D and that the Class II SMases D contain an additional intra-chain disulphide bridge (Cys53-Cys201). Structural analysis suggests that the highly homologous enzyme from Loxosceles bonetti is unable to hydrolyze sphingomyelin due to the 95G1y -> Asn and 134Pro -> Glu mutations that modify the local charge and hydrophobicity of the interfacial face. Structural and sequence comparisons confirm the evolutionary relationship between sphingomyelinases D and the glicerophosphodiester phosphoesterases which utilize a similar catalytic mechanism. (c) 2006 Elsevier B.V. All rights reserved.en
dc.description.affiliationUNESP, IBILCE, Dept Phys, Sao Jose do Rio Preto, SP, Brazil
dc.description.affiliationInstituto Butantan, Immunochem Lab, São Paulo, Brazil
dc.description.affiliationRAS, Inst Prot Res, Moscow 117901, Russia
dc.description.affiliationUniv Hamburg, Div Biochem & Mol Biol, Hamburg, Germany
dc.description.affiliationInstituto Butantan, Ctr Appl Toxicol, São Paulo, Brazil
dc.description.affiliationUnespUNESP, IBILCE, Dept Phys, Sao Jose do Rio Preto, SP, Brazil
dc.format.extent323-329
dc.identifierhttp://dx.doi.org/10.1016/j.bbrc.2006.01.123
dc.identifier.citationBiochemical and Biophysical Research Communications. San Diego: Academic Press Inc. Elsevier B.V., v. 342, n. 1, p. 323-329, 2006.
dc.identifier.doi10.1016/j.bbrc.2006.01.123
dc.identifier.issn0006-291X
dc.identifier.lattes9162508978945887
dc.identifier.orcid0000-0003-2460-1145
dc.identifier.urihttp://hdl.handle.net/11449/21992
dc.identifier.wosWOS:000235793800044
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofBiochemical and Biophysical Research Communications
dc.relation.ispartofjcr2.559
dc.rights.accessRightsAcesso restrito
dc.sourceWeb of Science
dc.subjectSphingomyelinase Dpt
dc.subjectcatalytic mechanismpt
dc.subjectMg2+-binding sitept
dc.subjecthydrodynamic behaviorpt
dc.subjectCrystal structurept
dc.subjectglycerophosphodiester phosphodiesterasespt
dc.titleStructural insights into the catalytic mechanism of sphingomyelinases D and evolutionary relationship to glycerophosphodiester phosphodiesterasesen
dc.typeArtigo
dcterms.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dcterms.rightsHolderElsevier B.V.
unesp.author.lattes9162508978945887[7]
unesp.author.orcid0000-0002-0405-8010[1]
unesp.author.orcid0000-0003-4221-9580[2]
unesp.author.orcid0000-0003-1016-5936[4]
unesp.author.orcid0000-0003-2460-1145[7]
unesp.campusUniversidade Estadual Paulista (Unesp), Instituto de Biociências Letras e Ciências Exatas, São José do Rio Pretopt

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