Molecular dynamic simulations and QM/MM studies addressed to build an active Tryptophan Synthase model. A critical enzyme to treat tuberculosis

• Type: Article in International Conference Proceedings Book
• Date: 2019

Authors

Teixeira, CSS (Author) Other; Sergio Filipe Sousa (Author) FCUP; Nuno M F S A Cerqueira (Author) FCUP

Conference proceedings International

Title: 6th IEEE Portuguese Meeting on Bioengineering, ENBENG 2019 - Proceedings

6th IEEE Portuguese Meeting on Bioengineering, ENBENG 2019

22 February 2019 through 23 February 2019

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Scopus - 1 Citation

Other information

Authenticus ID: P-00Q-K2Y

DOI: 10.1109/enbeng.2019.8692492

Abstract (EN): The latest data from the World Health Organization (WHO) underline the urgent need for the validation of new targets against tuberculosis (TB). Tryptophan Synthase (TSase) has been pointed has a good candidate, but its allosteric particularities turn it into a challenge both for experimentalists and for computational biochemists. In this study, molecular dynamic simulations and QM/MM studies were performed to build a closed conformation of a TSase model containing the substrate Indole-3-glycerolphosphate (IGP) in the a-active site and the PLP in its external aldimine form in the beta-active site. The results have shown that there is a conserved water molecule in the alpha-active site of the enzyme that should be important for the catalytic process. The built model is stable and can be the basis for further studies.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 5