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


Autoria(s): Dias, MVB; Ely, F.; Canduri, F.; Pereira, J. F.; Basso, L. A.; Palma, Mario Sergio; de Azevedo, W. F.; Santos, D. S.
Contribuinte(s)

Universidade Estadual Paulista (UNESP)

Data(s)

20/05/2014

20/05/2014

01/11/2004

Resumo

The 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.

Formato

2003-2005

Identificador

http://dx.doi.org/10.1107/S0907444904019869

Acta Crystallographica Section D-biological Crystallography. Copenhagen: Blackwell Munksgaard, v. 60, p. 2003-2005, 2004.

0907-4449

http://hdl.handle.net/11449/19411

10.1107/S0907444904019869

WOS:000224595200012

Idioma(s)

eng

Publicador

Blackwell Munksgaard

Relação

Acta Crystallographica Section D: Biological Crystallography

Direitos

closedAccess

Tipo

info:eu-repo/semantics/article