Crystallographic and spectroscopic characterization of a molecular hinge: Conformational changes in Bothropstoxin I, a dimeric Lys49- phospholipase A2 homologue

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Autor(es): dc.contributorUniversidade de São Paulo (USP)-
Autor(es): dc.contributorUniversidade Estadual Paulista (UNESP)-
Autor(es): dc.creatorDa Silva Giotto, M. T.-
Autor(es): dc.creatorGarratt, R. C.-
Autor(es): dc.creatorOliva, G.-
Autor(es): dc.creatorMascarenhas, Y. P.-
Autor(es): dc.creatorGiglio, J. R.-
Autor(es): dc.creatorCintra, A. C.O.-
Autor(es): dc.creatorDe Azevedo, W. F.-
Autor(es): dc.creatorArni, R. K.-
Autor(es): dc.creatorWard, R. J.-
Data de aceite: dc.date.accessioned2025-08-21T17:01:45Z-
Data de disponibilização: dc.date.available2025-08-21T17:01:45Z-
Data de envio: dc.date.issued2022-04-28-
Data de envio: dc.date.issued2022-04-28-
Data de envio: dc.date.issued1998-03-01-
Fonte completa do material: dc.identifierhttp://dx.doi.org/10.1002/(SICI)1097-0134(19980301)30:4<442-
Fonte completa do material: dc.identifierhttp://hdl.handle.net/11449/224091-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/11449/224091-
Descrição: dc.descriptionBothropstoxin I (BthTX-I) from the venom of Bothrops jararacussu is a myotoxic phospholipase A2 (PLA2) homologue which, although catalytically inactive due to an Asp49→Lys substitution, disrupts the integrity of lipid membranes by a Ca2+-independent mechanism. The crystal structures of two dimeric forms of BthTX-I which diffract X-rays to resolutions of 3.1 and 2.1 Å have been determined. The monomers in both structures are related by an almost perfect twofold axis of rotation and the dimer interfaces are defined by contacts between the N-terminal α-helical regions and the tips of the β- wings of partner monomers. Significant differences in the relative orientation of the monomers in the two crystal forms results in 'open'and 'closed' dimer conformations. Spectroscopic investigations of BthTX-I in solution have correlated these conformational differences with changes in the intrinsic fluorescence emission of the single tryptophan residues located at the dimer interface. The possible relevance of this structural transition in the Ca2+-independent membrane damaging activity is discussed.-
Descrição: dc.descriptionInstitute of Physics (IFSC) USP, São Carlos-SP-
Descrição: dc.descriptionDepartment of Biochemistry Faculty of Medicine USP, Ribeirão Preto-SP-
Descrição: dc.descriptionDepartment of Physics IBILCE-UNESP, Sao Jose do Rio Preto-SP-
Descrição: dc.descriptionDepartment of Biochemistry FMRP-USP, Avenida Bandeirantes 3900, CEP 14049-900, Ribeirao Preto-SP-
Descrição: dc.descriptionDepartment of Physics IBILCE-UNESP, Sao Jose do Rio Preto-SP-
Formato: dc.format442-454-
Idioma: dc.languageen-
Relação: dc.relationProteins: Structure, Function and Genetics-
???dc.source???: dc.sourceScopus-
Palavras-chave: dc.subjectProtein-membrane interaction-
Palavras-chave: dc.subjectQuaternary structural change-
Palavras-chave: dc.subjectSpectroscopy-
Palavras-chave: dc.subjectVenom toxin-
Palavras-chave: dc.subjectX-ray diffraction-
Título: dc.titleCrystallographic and spectroscopic characterization of a molecular hinge: Conformational changes in Bothropstoxin I, a dimeric Lys49- phospholipase A2 homologue-
Tipo de arquivo: dc.typelivro digital-
Aparece nas coleções:Repositório Institucional - Unesp

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