Crystallization and preliminary X-ray crystallographic analysis of chorismate synthase from Mycobacterium tuberculosis

dc.contributorUniversidade Estadual Paulista (Unesp)
dc.contributorUniversidade Federal do Rio Grande do Sul (UFRGS)
dc.contributorPontificia Univ Catolica Rio Grande do Sul
dc.date.accessioned2014-05-20T13:54:20Z
dc.date.available2014-05-20T13:54:20Z
dc.date.created2014-05-20T13:54:20Z
dc.date.issued2004-11-01
dc.identifierActa Crystallographica Section D-biological Crystallography. Copenhagen: Blackwell Munksgaard, v. 60, p. 2003-2005, 2004.
dc.identifier0907-4449
dc.identifierhttp://hdl.handle.net/11449/19411
dc.identifier10.1107/S0907444904019869
dc.identifierWOS:000224595200012
dc.identifier2901888624506535
dc.description.abstractThe enzymes of the shikimate pathway are potential targets for the development of new therapies because they are essential for bacteria but absent from mammals. The last step in this pathway is performed by chorismate synthase (CS), which catalyzes the conversion of 5-enolpyruvylshikimate-3-phosphate to chorismate. Optimization of crystallization trials allowed the crystallization of homogeneous recombinant CS from Mycobacterium tuberculosis (MtCS). The crystals of MtCS belong to space group P6(4)22 (or P6(2)22) and diffract to 2.8 Angstrom resolution, with unit-cell parameters a = b = 129.7, c = 156.8 Angstrom. There are two molecules in the asymmetric unit. Molecular-replacement trials were not sucessful. Heavy-atom derivative screening is in progress.
dc.languageeng
dc.publisherBlackwell Munksgaard
dc.relationActa Crystallographica Section D: Biological Crystallography
dc.rightsAcesso restrito
dc.sourceWeb of Science
dc.titleCrystallization and preliminary X-ray crystallographic analysis of chorismate synthase from Mycobacterium tuberculosis
dc.typeArtículos de revistas


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