Crystallization and preliminary X-ray crystallographic analysis of chorismate synthase from Mycobacterium tuberculosis.
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 A resolution, with unit-cell parameters a = b = 129.7, c = 156.8 A. There are two molecules in the asymmetric unit. Molecular-replacement trials were not successful. Heavy-atom derivative screening is in progress.
Dias
Marcio Viniciusbertacine
MV
Departamento de Física, UNESP, São José do Rio Preto, SP 15054-000, Brazil.
Ely
Fernanda
F
Canduri
Fernanda
F
Pereira
José Henrique
JH
Frazzon
Jeverson
J
Basso
Luiz Augusto
LA
Palma
Mário Sérgio
MS
de Azevedo
Walter Filgueira
WF
Santos
Diógenes Santiago
DS
D003460:Crystallization; D018360:Crystallography, X-Ray; D009169:Mycobacterium tuberculosis / Q000201:enzymology*; D019761:Phosphorus-Oxygen Lyases / Q000737:chemistry*
C019895:chorismate synthase; D019761:Phosphorus-Oxygen Lyases