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