Effects of the magnesium and chloride ions and shikimate on the structure of shikimate kinase from Mycobacterium tuberculosis

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dc.contributor.authorBertacine Dias, Marcio Vinicius
dc.contributor.authorFaim, Livia Maria
dc.contributor.authorVasconcelos, Igor Bordin
dc.contributor.authorde Oliveira, Jaim Simoes
dc.contributor.authorBasso, Luiz Augusto
dc.contributor.authorSantos, Diogenes Santiago
dc.contributor.authorde Azevedo, Walter Filgueira
dc.contributor.institutionPontificia Univ Catolica Rio Grande Sul
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.date.accessioned2014-05-20T15:28:34Z
dc.date.available2014-05-20T15:28:34Z
dc.date.issued2007-01-01
dc.description.abstractBacteria, fungi and plants can convert carbohydrate and phosphoenolpyruvate into chorismate, which is the precursor of various aromatic compounds. The seven enzymes of the shikimate pathway are responsible for this conversion. Shikimate kinase (SK) is the fifth enzyme in this pathway and converts shikimate to shikimate-3-phosphate. In this work, the conformational changes that occur on binding of shikimate, magnesium and chloride ions to SK from Mycobacterium tuberculosis (MtSK) are described. It was observed that both ions and shikimate influence the conformation of residues of the active site of MtSK. Magnesium influences the conformation of the shikimate hydroxyl groups and the position of the side chains of some of the residues of the active site. Chloride seems to influence the affinity of ADP and its position in the active site and the opening length of the LID domain. Shikimate binding causes a closing of the LID domain and also seems to influence the crystallographic packing of SK. The results shown here could be useful for understanding the catalytic mechanism of SK and the role of ions in the activity of this protein.en
dc.description.affiliationPontificia Univ Catolica Rio Grande Sul, Ctr Pesquisa Biol Mol & Funct, BR-90619900 Porto Alegre, RS, Brazil
dc.description.affiliationUNESP, Dept Fis, Programa PosGraduacao Biofis Mol, BR-15054000 Sao Jose do Rio Preto, SP, Brazil
dc.description.affiliationPontificia Univ Catolica Rio Grande Sul, Fac Biociencias, BR-90619900 Porto Alegre, RS, Brazil
dc.description.affiliationUnespUNESP, Dept Fis, Programa PosGraduacao Biofis Mol, BR-15054000 Sao Jose do Rio Preto, SP, Brazil
dc.format.extent1-6
dc.identifierhttp://dx.doi.org/10.1107/S1744309106046823
dc.identifier.citationActa Crystallographica Section F-structural Biology and Crystallization Communications. Oxford: Blackwell Publishing, v. 63, p. 1-6, 2007.
dc.identifier.doi10.1107/S1744309106046823
dc.identifier.issn1744-3091
dc.identifier.urihttp://hdl.handle.net/11449/38353
dc.identifier.wosWOS:000243010400001
dc.language.isoeng
dc.publisherBlackwell Publishing
dc.relation.ispartofActa Crystallographica Section F: Structural Biology and Crystallization Communications
dc.rights.accessRightsAcesso restrito
dc.sourceWeb of Science
dc.titleEffects of the magnesium and chloride ions and shikimate on the structure of shikimate kinase from Mycobacterium tuberculosisen
dc.typeArtigo
dcterms.licensehttp://olabout.wiley.com/WileyCDA/Section/id-406071.html
dcterms.rightsHolderBlackwell Publishing
unesp.author.orcid0000-0002-5312-0191[1]
unesp.author.orcid0000-0003-4971-463X[6]
unesp.author.orcid0000-0003-0903-2407[5]
unesp.campusUniversidade Estadual Paulista (Unesp), Instituto de Biociências Letras e Ciências Exatas, São José do Rio Pretopt

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