| Full text | |
| Author(s): |
Dias, Marcio Vinicius Bertacine
;
Ely, Fernanda
;
Canduri, Fernanda
;
Pereira, José Henrique
;
Frazzon, Jeverson
;
Basso, Luiz Augusto
;
Palma, Mário Sérgio
;
Azevedo Junior, Walter Filgueira de
[8]
;
Santos, Diógenes Santiago
Total Authors: 9
|
| Document type: | Journal article |
| Source: | ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY; v. 60, n. 11, p. 2003-2005, Nov. 2004. |
| Field of knowledge: | Biological Sciences - Biophysics |
| Abstract | |
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. (AU) | |
| FAPESP's process: | 01/07532-0 - Structural genomics of cyclin dependent kinases and plant defensive proteinases and their natural inhibitors |
| Grantee: | Walter Filgueira de Azevedo Junior |
| Support Opportunities: | Regular Research Grants |