Structural bioinformatics study of EPSP synthase from Mycobacterium tuberculosis

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dc.contributor.authorPereira, J. H.
dc.contributor.authorCanduri, F.
dc.contributor.authorde Oliveira, J. S.
dc.contributor.authorda Silveira, NJF
dc.contributor.authorBasso, L. A.
dc.contributor.authorPalma, Mario Sergio [UNESP]
dc.contributor.authorde Azevedo, W. F.
dc.contributor.authorSantos, D. S.
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionInstituto Butantan
dc.contributor.institutionUniversidade Federal do Rio Grande do Sul (UFRGS)
dc.contributor.institutionPontificia Univ Catolica Rio Grande do Sul
dc.date.accessioned2014-05-20T13:54:19Z
dc.date.available2014-05-20T13:54:19Z
dc.date.issued2003-12-19
dc.description.abstractThe shikimate pathway is an attractive target for herbicides and antimicrobial agent development because it is essential in algae, higher plants, bacteria, and fungi, but absent from mammals. Homologues to enzymes in the shikimate pathway have been identified in the genome sequence of Mycobacterium tuberculosis. Among them, the EPSP synthase was proposed to be present by sequence homology. Accordingly, in order to pave the way for structural and functional efforts towards anti-mycobacterial agent development, here we describe the molecular modeling of 5-enolpyruvylshikimate-3-phosphate (EPSP) synthase isolated from M. tuberculosis that should provide a structural framework on which the design of specific inhibitors may be based on. Significant differences in the relative orientation of the domains in the two models result in open and closed conformations. The possible relevance of this structural transition in the ligand biding is discussed. (C) 2003 Elsevier B.V. All rights reserved.en
dc.description.affiliationUNESP, Dept Fis, BR-15054000 Sao Jose do Rio Preto, SP, Brazil
dc.description.affiliationInst Butantan, Ctr Appl Toxinol, BR-05503900 São Paulo, SP, Brazil
dc.description.affiliationUFRGS, Dept Biol Mol & Biotecnol, Rede Brasileira Pesquisa Pesquisa TB Grp Microbio, BR-91501970 Porto Alegre, RS, Brazil
dc.description.affiliationUNESP, CEIS, Dept Biol, Inst Biosci,Lab Struct Biol & Zoochem, BR-13506900 Rio Claro, SP, Brazil
dc.description.affiliationPontificia Univ Catolica Rio Grande do Sul, Fac Farm, Inst Pesquisas Biomed, Porto Alegre, RS, Brazil
dc.description.affiliationUnespUNESP, Dept Fis, BR-15054000 Sao Jose do Rio Preto, SP, Brazil
dc.description.affiliationUnespUNESP, CEIS, Dept Biol, Inst Biosci,Lab Struct Biol & Zoochem, BR-13506900 Rio Claro, SP, Brazil
dc.format.extent608-614
dc.identifierhttp://dx.doi.org/10.1016/j.bbrc.2003.10.175
dc.identifier.citationBiochemical and Biophysical Research Communications. San Diego: Academic Press Inc. Elsevier B.V., v. 312, n. 3, p. 608-614, 2003.
dc.identifier.doi10.1016/j.bbrc.2003.10.175
dc.identifier.issn0006-291X
dc.identifier.lattes2901888624506535
dc.identifier.urihttp://hdl.handle.net/11449/19408
dc.identifier.wosWOS:000187021300011
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.subjectEPSP synthasept
dc.subjectbioinformaticspt
dc.subjectmolecular modelingpt
dc.subjectMycobacterium tuberculosispt
dc.titleStructural bioinformatics study of EPSP synthase from Mycobacterium tuberculosisen
dc.typeArtigo
dcterms.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dcterms.rightsHolderElsevier B.V.
unesp.author.lattes2901888624506535
unesp.author.orcid0000-0002-7363-8211[6]
unesp.author.orcid0000-0003-0903-2407[5]
unesp.author.orcid0000-0003-4971-463X[8]
unesp.campusUniversidade Estadual Paulista (Unesp), Instituto de Biociências, Rio Claropt
unesp.campusUniversidade Estadual Paulista (Unesp), Instituto de Biociências Letras e Ciências Exatas, São José do Rio Pretopt

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Artigos - Física - IBILCE
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