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dc.contributor.authorVaso, Alessandra [UNESP]
dc.contributor.authordos Santos, Diogenes S.
dc.contributor.authorBasso, Luis Augusto
dc.contributor.authorPalma, Mario Sergio [UNESP]
dc.date.accessioned2014-05-20T13:55:28Z
dc.date.available2014-05-20T13:55:28Z
dc.date.issued2011-04-30
dc.identifierhttp://dx.doi.org/10.1016/j.ijms.2010.06.002
dc.identifier.citationInternational Journal of Mass Spectrometry. Amsterdam: Elsevier B.V., v. 302, n. 1-3, p. 12-18, 2011.
dc.identifier.issn1387-3806
dc.identifier.urihttp://hdl.handle.net/11449/19851
dc.description.abstractThe enzyme 5-enolpyruvylshikimate-3-phosphate synthase (EPSPS) catalyzes the reaction between shikimate-3-phosphate (S3P) and phosphoenolpyruvate (PEP) to form 5-enolpyruvylshikimate-3-phosphate, an intermediate in the shikimate pathway, which leads to the biosynthesis of aromatic amino acids. The two-domain structure of EPSPS is formed by a 6-fold replication of protein folding units, each one formed by two parallel a-helices and four-stranded beta-sheets. The apo form of the enzyme exists in an open conformation, but when bound to PEP, the EPSPS conformation is closed. The H/D exchange properties of EPSPS from Mycobacterium tuberculosis (Mt) were studied for both enzyme conformations using ESI-mass spectrometry. We mapped the identified H/D exchange sites on the 3D structure. H/D exchange revealed that the enzyme undergoes extensive conformational change upon forming the PEP complex, which seem to favor solvent access at domain 1, while they partially prevent solvent access to domain 2. This may be part of the catalysis mechanism of the enzyme, stabilizing S3P binding and inducing cleft closure, which controls the entrance of substrate molecules. (C) 2010 Elsevier B.V. All rights reserved.en
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.sponsorshipMillennium Institute
dc.description.sponsorshipFinanciadora de Estudos e Projetos (FINEP)
dc.format.extent12-18
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofInternational Journal of Mass Spectrometry
dc.sourceWeb of Science
dc.subjectESI-MSen
dc.subjectH/D exchangeen
dc.subjectMass spectrometryen
dc.subjectProteins dynamicsen
dc.subjectShikimate pathwayen
dc.titleHydrogen/deuterium exchange mass spectrometry for characterizing phosphoenolpyruvate-induced structural transitions in Mycobacterium tuberculosis 5-enolpyruvylshikimate-3-phosphate synthase (EC 2.5.1.1)en
dc.typeArtigo
dcterms.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dcterms.rightsHolderElsevier B.V.
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionPontifícia Universidade Católica do Rio Grande do Sul (PUCRS)
dc.description.affiliationUNESP, Inst Biosci, Lab Struct Biol & Zoochem, CEIS Dept Biol, BR-13506900 Rio Claro, SP, Brazil
dc.description.affiliationCtr Pesquisas Biol Mol & Func PUCRS, BR-90619900 Porto Alegre, RS, Brazil
dc.description.affiliationUnespUNESP, Inst Biosci, Lab Struct Biol & Zoochem, CEIS Dept Biol, BR-13506900 Rio Claro, SP, Brazil
dc.identifier.doi10.1016/j.ijms.2010.06.002
dc.identifier.wosWOS:000290693800003
dc.rights.accessRightsAcesso restrito
dc.description.sponsorshipIdFAPESP: 06/57122-7
unesp.campusUniversidade Estadual Paulista (Unesp), Instituto de Biociências, Rio Claropt
dc.identifier.lattes2901888624506535
unesp.author.lattes2901888624506535
unesp.author.orcid0000-0003-0903-2407[3]
unesp.author.orcid0000-0002-7363-8211[4]
dc.relation.ispartofjcr1.826
dc.relation.ispartofsjr0,610
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