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Interaction of shikimic acid with shikimate kinase (Retracted Article. See vol 334, pg 967, 2005)

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dc.contributor.authorPereira, J. H.
dc.contributor.authorde Oliveira, J. S.
dc.contributor.authorCanduri, F.
dc.contributor.authorDias, MVB
dc.contributor.authorPalma, Mario Sergio [UNESP]
dc.contributor.authorBasso, L. A.
dc.contributor.authorde Azevedo, W. F.
dc.contributor.authorSantos, D. S.
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionUniversidade Federal do Rio Grande do Sul (UFRGS)
dc.contributor.institutionCtr Appl Toxinol
dc.contributor.institutionPontificia Univ Catolica Rio Grande do Sul
dc.date.accessioned2014-05-20T13:54:29Z
dc.date.available2014-05-20T13:54:29Z
dc.date.issued2004-12-03
dc.description.abstractThe crystal structure of shikimate kinase from Mycobacterium tuberculosis (MtSK) complexed with MgADP and shikimic acid (shikimate) has been determined at 2.3 Angstrom resolution, clearly revealing the amino acid residues involved in shikimate binding. In MtSK, the Glu61 strictly conserved in SK forms a hydrogen bond and salt-bridge with Arg58 and assists in positioning the guanidinium group of Arg58 for shikimate binding. The carboxyl group of shikimate interacts with Arg58, Gly81, and Arg136, and hydroxyl groups with Asp34 and Gly80. The crystal structure of MtSK-MgADP-shikimate will provide crucial information for elucidation of the mechanism of SK-catalyzed reaction and for the development of a new generation of drugs against tuberculosis. (C) 2004 Elsevier B.V. All rights reserved.en
dc.description.affiliationUNESP, Dept Phys, BR-15054000 Sao Jose do Rio Preto, SP, Brazil
dc.description.affiliationUniv Fed Rio Grande do Sul, Dept Biol Mol & Biotecnol, Rede Brasileira Pesquisa Tuberculose Grp Microbio, BR-91501970 Porto Alegre, RS, Brazil
dc.description.affiliationCtr Appl Toxinol, Inst Butantan, BR-05503900 São Paulo, Brazil
dc.description.affiliationUNESP, Lab Struct Biol & Zoochem, CEIS, Dept Biol,Inst Biosci, BR-13506900 Rio Claro, SP, Brazil
dc.description.affiliationPontificia Univ Catolica Rio Grande do Sul, Ctr Pesquisa & Desenvolvimento Biol Mol & Func, BR-90619900 Porto Alegre, RS, Brazil
dc.description.affiliationUnespUNESP, Dept Phys, BR-15054000 Sao Jose do Rio Preto, SP, Brazil
dc.description.affiliationUnespUNESP, Lab Struct Biol & Zoochem, CEIS, Dept Biol,Inst Biosci, BR-13506900 Rio Claro, SP, Brazil
dc.format.extent10-17
dc.identifierhttp://dx.doi.org/10.1016/j.bbrc.2004.09.217
dc.identifier.citationBiochemical and Biophysical Research Communications. San Diego: Academic Press Inc. Elsevier B.V., v. 325, n. 1, p. 10-17, 2004.
dc.identifier.doi10.1016/j.bbrc.2004.09.217
dc.identifier.issn0006-291X
dc.identifier.lattes2901888624506535
dc.identifier.urihttp://hdl.handle.net/11449/19485
dc.identifier.wosWOS:000225173400003
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.subjectdrug designpt
dc.subjectMycobacterium tuberculosispt
dc.subjectshikimate kinasept
dc.subjectStructurept
dc.subjectshikimic acidpt
dc.titleInteraction of shikimic acid with shikimate kinase (Retracted Article. See vol 334, pg 967, 2005)en
dc.typeArtigo
dcterms.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dcterms.rightsHolderElsevier B.V.
dspace.entity.typePublication
unesp.author.lattes2901888624506535
unesp.author.orcid0000-0002-5312-0191[4]
unesp.author.orcid0000-0003-0903-2407[6]
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
unesp.departmentBiologia - IBpt
unesp.departmentFísica - IBILCEpt

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São José do Rio Preto - IBILCE - Instituto de Biociências, Letras e Ciências Exatas
Rio Claro - IB - Instituto de Biociências