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© Institut Pasteur
Cells infected for 24 hrs with C. Trachomatis. The cell nuclei are labelled in blue, the bacteria appear yellow, within the inclusion lumen. A bacterial protein secreted out the inclusion into the host cytoplasm id labelled in red.
Publication : Biochemical and biophysical research communications

Identification of a non-competitive inhibitor of Plasmodium falciparum aspartate transcarbamoylase.

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Biochemical and biophysical research communications - 11 Mar 2018

Lunev S, Bosch SS, Batista FA, Wang C, Li J, Linzke M, Kruithof P, Chamoun G, Dömling ASS, Wrenger C, Groves MR,

Link to Pubmed [PMID] – 29476738

Link to DOI – S0006-291X(18)30341-310.1016/j.bbrc.2018.02.112

Biochem Biophys Res Commun 2018 03; 497(3): 835-842

Aspartate transcarbamoylase catalyzes the second step of de-novo pyrimidine biosynthesis. As malarial parasites lack pyrimidine salvage machinery and rely on de-novo production for growth and proliferation, this pathway is a target for drug discovery. Previously, an apo crystal structure of aspartate transcarbamoylase from Plasmodium falciparum (PfATC) in its T-state has been reported. Here we present crystal structures of PfATC in the liganded R-state as well as in complex with the novel inhibitor, 2,3-napthalenediol, identified by high-throughput screening. Our data shows that 2,3-napthalediol binds in close proximity to the active site, implying an allosteric mechanism of inhibition. Furthermore, we report biophysical characterization of 2,3-napthalenediol. These data provide a promising starting point for structure based drug design targeting PfATC and malarial de-novo pyrimidine biosynthesis.

https://pubmed.ncbi.nlm.nih.gov/29476738