engleski

Parametrization of the manganese binding sites of the Mycobacterium tuberculosis transcriptional regulator MntR

Manganese homeostasis in the bacterium Mycobacterium tuberculosis is regulated by MntR, a homodimeric protein in which each monomer harbors a binuclear and a mononuclear manganese binding site (Figure 1). [1] Dynamic behaviors of proteins can be studied at the atomic level using classical molecular dynamics. There are multiple approaches to modeling metal-protein interactions within molecular dynamics simulations. We modeled the manganese binding sites of MntR using different strategies and ran molecular dynamics simulations of the parametrized systems. The interaction was first modeled using a simple non-bonded model. Next, we extracted parameters for the bonded model using interpolation from the manganese parameter database. [2] Finally, we developed parameters for the bonded model using the approach described by Li et al. [3] Manganese binding sites modeled by all of the aforementioned approaches were lastly compared. This work was supported by the Croatian Science Foundation project “Manganese metallosensors” IP-2020-02- 3446.

manganese ion, transcription factors, parametrization

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