Structural bioinformatics study of EPSP synthase from Mycobacterium tuberculosis
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Data
2003-12-19
Autores
Pereira, J. H.
Canduri, F.
de Oliveira, J. S.
da Silveira, NJF
Basso, L. A.
Palma, Mario Sergio [UNESP]
de Azevedo, W. F.
Santos, D. S.
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Editor
Elsevier B.V.
Resumo
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. (C) 2003 Elsevier B.V. All rights reserved.
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EPSP synthase, bioinformatics, molecular modeling, Mycobacterium tuberculosis
Como citar
Biochemical and Biophysical Research Communications. San Diego: Academic Press Inc. Elsevier B.V., v. 312, n. 3, p. 608-614, 2003.