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dc.contributor.authorOliveira, Isadora A
dc.contributor.authorGoncalves, Arlan S
dc.contributor.authorNeves, Jorge L
dc.contributor.authorvon Itzstein, Mark
dc.contributor.authorTodeschini, Adriane R
dc.date.accessioned2017-05-03T15:56:15Z
dc.date.available2017-05-03T15:56:15Z
dc.date.issued2014
dc.identifier.issn0021-9258
dc.identifier.doi10.1074/jbc.M112.399303
dc.identifier.urihttp://hdl.handle.net/10072/67771
dc.description.abstractTrypanosoma cruzi trans-sialidase (TcTS) is a key target protein for Chagas disease chemotherapy. In this study, we investigated the implications of active site flexibility on the biochemical mechanism of TcTS. Molecular dynamics studies revealed remarkable plasticity in the TcTS catalytic site, demonstrating, for the first time, how donor substrate engagement with the enzyme induces an acceptor binding site in the catalytic pocket that was not previously captured in crystal structures. Furthermore, NMR data showed cooperative binding between donor and acceptor substrates, supporting theoretical results. In summary, our data put forward a coherent dynamic framework to understand how a glycosidase evolved its highly efficient trans-glycosidase activity.
dc.description.peerreviewedYes
dc.description.publicationstatusYes
dc.languageEnglish
dc.language.isoeng
dc.publisherThe American Society for Biochemistry and Molecular Biology Inc
dc.publisher.placeUnited States
dc.relation.ispartofstudentpublicationN
dc.relation.ispartofpagefrom423
dc.relation.ispartofpageto436
dc.relation.ispartofissue1
dc.relation.ispartofjournalJournal of Biological Chemistry
dc.relation.ispartofvolume289
dc.rights.retentionY
dc.subject.fieldofresearchChemical sciences
dc.subject.fieldofresearchProteins and peptides
dc.subject.fieldofresearchBiological sciences
dc.subject.fieldofresearchBiomedical and clinical sciences
dc.subject.fieldofresearchcode34
dc.subject.fieldofresearchcode340407
dc.subject.fieldofresearchcode31
dc.subject.fieldofresearchcode32
dc.titleEvidence of Ternary Complex Formation in Trypanosoma cruzi trans-Sialidase Catalysis
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
gro.hasfulltextNo Full Text
gro.griffith.authorvon Itzstein, Mark


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