Abstract

Purine phosphoribosyltransferases are members of a group of enzymes that are responsible for the formation of purine, pyrimidine and pyridine nucleotides. One feature of this family is a flexible loop, which is involved in the catalytic mechanism. This loop is variable both in sequence and structure in the phosphoribosyltransferase family. This paper describes the modelling and validation of a model of Plasmodium falciparum hypoxanthine-guanidine- phosphoribosyltransferase in an open conformation. A comparison of this model with 3D-structures of other members of the phosphorybosyl-transferase family has allowed an assessment of the role of the open and closed conformations of the loop in the catalytic mechanism.