Crystallization and preliminary X-ray diffraction analysis of an l-amino-acid oxidase from Bothrops jararacussu venom

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dc.contributor.authorUllah, Anwar [UNESP]
dc.contributor.authorCoronado, Monika [UNESP]
dc.contributor.authorMurakami, Mario T.
dc.contributor.authorBetzel, Christian
dc.contributor.authorArni, Raghuvir K. [UNESP]
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionCtr Nacl Pesquisa Energia & Mat
dc.contributor.institutionUniv Hamburg
dc.date.accessioned2014-05-20T14:02:42Z
dc.date.available2014-05-20T14:02:42Z
dc.date.issued2012-02-01
dc.description.abstractSnake-venom l-amino-acid oxidases (SV-LAAOs) trigger a wide range of local and systematic effects, including inhibition of platelet aggregation, cytotoxicity, haemolysis, apoptosis and haemorrhage. These effects mainly arise from the uncontrolled release of the hydrogen peroxide that is produced by the redox reaction involving l-amino acids catalyzed by these flavoenzymes. Taking their clinical relevance into account, few SV-LAAOs have been structurally characterized and the structural determinants responsible for their broad direct and indirect pharmacological activities remain unclear. In this work, an LAAO from Bothrops jararacussu venom (BJu-LAAO) was purified and crystallized. The BJu-LAAO crystals belonged to space group P21, with unit-cell parameters a similar to=similar to 66.38, b = 72.19, c = 101.53 angstrom, beta = 90.9 degrees. The asymmetric unit contained two similar to molecules and the structure was determined and partially refined at 3.0 angstrom resolution.en
dc.description.affiliationUniv Estadual Paulista UNESP, Dept Fis, Ctr Multiusuario Inovacao Biomol, BR-15054000 Sao Jose do Rio Preto, SP, Brazil
dc.description.affiliationCtr Nacl Pesquisa Energia & Mat, LNBio, BR-13083970 Campinas, SP, Brazil
dc.description.affiliationUniv Hamburg, Inst Biochem & Mol Biol, Lab Struct Biol Infect, D-22603 Hamburg, Germany
dc.description.affiliationUnespUniv Estadual Paulista UNESP, Dept Fis, Ctr Multiusuario Inovacao Biomol, BR-15054000 Sao Jose do Rio Preto, SP, Brazil
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.description.sponsorshipCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.description.sponsorshipDeutscher Akademischer Austauschdienst (DAAD)
dc.description.sponsorshipTWAS
dc.format.extent211-213
dc.identifierhttp://dx.doi.org/10.1107/S1744309111054923
dc.identifier.citationActa Crystallographica Section F-structural Biology and Crystallization Communications. Hoboken: Wiley-blackwell, v. 68, p. 211-213, 2012.
dc.identifier.doi10.1107/S1744309111054923
dc.identifier.fileWOS000299948000023.pdf
dc.identifier.issn1744-3091
dc.identifier.lattes9162508978945887
dc.identifier.orcid0000-0003-2460-1145
dc.identifier.urihttp://hdl.handle.net/11449/22102
dc.identifier.wosWOS:000299948000023
dc.language.isoeng
dc.publisherWiley-Blackwell
dc.relation.ispartofActa Crystallographica Section F: Structural Biology and Crystallization Communications
dc.rights.accessRightsAcesso restrito
dc.sourceWeb of Science
dc.subjectl-amino acid oxidaseen
dc.subjectSnake venomen
dc.titleCrystallization and preliminary X-ray diffraction analysis of an l-amino-acid oxidase from Bothrops jararacussu venomen
dc.typeArtigo
dcterms.licensehttp://journals.iucr.org/services/copyrightpolicy.html
dcterms.rightsHolderWiley-blackwell
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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Artigos - Física - IBILCE