LOW-FREQUENCY MOTIONS IN PHOSPHOGLYCERATE KINASE - A NORMAL-MODE ANALYSIS

This paper presents a normal mode analysis of yeast Phosphoglycerate k inase, whose goal is to study the large amplitude collective motions o f this protein. It is constituted of two globular domains, and many au thors have proposed that domains have a relative movement between them in order to allow the phosphoryl transfer reaction. Our results show that the lowest frequency modes, below 5 cm(-1), contribute the most t o the hinge bending motions of the N- and C-terminal domains. We found three types of movements, which are a twist propeller motion, a sciss ors type hinge motion, and a shear motion between the domains. We pres ent the local conformational variations which are coupled to the domai n motions. The thermal atomic fluctuations at 300 K and the correlatio ns between them, are also analyzed.