The structure of Plasmodium falciparum serine hydroxymethyltransferase reveals a novel redox switch that regulates its activities

• Main Authors: Penchit Chitnumsub, Wanwipa Ittarat, Aritsara Jaruwat, Krittikar Noytanom, Watcharee Amornwatcharapong, Wichai Pornthanakasem, Pimchai Chaiyen, Yongyuth Yuthavong, Ubolsree Leartsakulpanich
• Other Authors: Thailand National Center for Genetic Engineering and Biotechnology
• Format: Article
• Published: 2018
• Subjects: Biochemistry, Genetics and Molecular Biology; Medicine
• Online Access: https://repository.li.mahidol.ac.th/handle/123456789/33357
• Institution: Mahidol University

Plasmodium falciparum serine hydroxymethyltransferase (PfSHMT), an enzyme in the dTMP synthesis cycle, is an antimalarial target because inhibition of its expression or function has been shown to be lethal to the parasite. As the wild-type enzyme could not be crystallized, protein engineering of res...