A structural model for chorismate synthase from Mycobacterium tuberculosis in complex with coenzyme and substrate.

Cláudia Lemelle Fernandes; Ardala Breda; Diógenes Santiago Santos; Luiz Augusto Basso; Osmar Norberto de Souza

doi:10.1016/j.compbiomed.2006.01.001

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A structural model for chorismate synthase from Mycobacterium tuberculosis in complex with coenzyme and substrate.

Cláudia Lemelle Fernandes·Ardala Breda·Diógenes Santiago Santos·Luiz Augusto Basso·Osmar Norberto de Souza

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Abstract

The enzymes of the shikimate pathway constitute an excellent target for the design of new antibacterial agents; chorismate synthase (CS) catalyzes the last step of this pathway. The prediction of Mycobacterium tuberculosis (MTB) CS three-dimensional structure and the geometric docking of the coenzyme FMN and the substrate EPSP were performed using the crystal structure of CS from Streptococcus pneumoniae as template. Energy minimization of the whole complex showed, as expected, that most of the template interactions are preserved in the MTB structure, except for HIS11, ARG139 and GLN255. However, novel interactions involving ARG111, GLY113 and SER317 were also observed.

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Amino Acid Sequence Coenzymes Flavin Mononucleotide Models, Molecular Molecular Sequence Data Mycobacterium tuberculosis Phosphorus-Oxygen Lyases Sequence Homology, Amino Acid Substrate Specificity Journal Article Research Support, Non-U.S. Gov't

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Cláudia Lemelle Fernandes, Ardala Breda, Diógenes Santiago Santos, Luiz Augusto Basso, Osmar Norberto de Souza. 2006-04-11. A structural model for chorismate synthase from Mycobacterium tuberculosis in complex with coenzyme and substrate.. https://doi.org/10.1016/j.compbiomed.2006.01.001

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