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Please use this identifier to cite or link to this item: http://acervodigital.unesp.br/handle/11449/19485
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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-
dc.contributor.authorBasso, L. A.-
dc.contributor.authorde Azevedo, W. F.-
dc.contributor.authorSantos, D. S.-
dc.date.accessioned2014-05-20T13:54:29Z-
dc.date.accessioned2016-10-25T17:04:37Z-
dc.date.available2014-05-20T13:54:29Z-
dc.date.available2016-10-25T17:04:37Z-
dc.date.issued2004-12-03-
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.issn0006-291X-
dc.identifier.urihttp://hdl.handle.net/11449/19485-
dc.identifier.urihttp://acervodigital.unesp.br/handle/11449/19485-
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.format.extent10-17-
dc.language.isoeng-
dc.publisherElsevier B.V.-
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dc.titleInteraction of shikimic acid with shikimate kinase (Retracted Article.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.typeoutro-
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.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.identifier.doi10.1016/j.bbrc.2004.09.217-
dc.identifier.wosWOS:000225173400003-
dc.rights.accessRightsAcesso restrito-
dc.relation.ispartofBiochemical and Biophysical Research Communications-
Appears in Collections:Artigos, TCCs, Teses e Dissertações da Unesp

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