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Structural bioinformatics study of EPSP synthase from Mycobacterium tuberculosis.

Authors
  • Pereira, José Henrique
  • Canduri, Fernanda
  • de Oliveira, Jaim Simões
  • da Silveira, Nelson José Freitas
  • Basso, Luiz Augusto
  • Palma, Mário Sérgio
  • de Azevedo, Walter Filgueira Jr
  • Santos, Diógenes Santiago
Type
Published Article
Journal
Biochemical and biophysical research communications
Publication Date
Dec 19, 2003
Volume
312
Issue
3
Pages
608–614
Identifiers
PMID: 14680808
Source
Medline
License
Unknown

Abstract

The shikimate pathway is an attractive target for herbicides and antimicrobial agent development because it is essential in algae, higher plants, bacteria, and fungi, but absent from mammals. Homologues to enzymes in the shikimate pathway have been identified in the genome sequence of Mycobacterium tuberculosis. Among them, the EPSP synthase was proposed to be present by sequence homology. Accordingly, in order to pave the way for structural and functional efforts towards anti-mycobacterial agent development, here we describe the molecular modeling of 5-enolpyruvylshikimate-3-phosphate (EPSP) synthase isolated from M. tuberculosis that should provide a structural framework on which the design of specific inhibitors may be based on. Significant differences in the relative orientation of the domains in the two models result in "open" and "closed" conformations. The possible relevance of this structural transition in the ligand biding is discussed.

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