Exploring the structural assembly of rice ADP-glucose pyrophosphorylase subunits using MD simulation.

ABSTRACT

ADP-glucose pyrophosphorylase plays a pivotal role as an allosteric enzyme, essential for starch biosynthesis in plants. The higher plant AGPase comparises of a pair of large and a pair of small subunits to form a heterotetrameric complex. Growing evidence indicates that each subunit plays a distinct role in regulating the underlying mechanism of starch biosynthesis. In the rice genome, there are four large subunit genes (OsL1-L4) and three small subunit genes (OsS1, OsS2a, and OsS2b). While the structural assembly of cytosolic rice AGPase subunits (OsL2OsS2b) has been elucidated, there is currently no such documented research available for plastidial rice AGPases (OsL1OsS1). In this study, we employed protein modeling and MD simulation approaches to gain insights into the structural association of plastidial rice AGPase subunits. Our results demonstrate that the heterotetrameric association of OsL1OsS1 is very similar to that of cytosolic OsL2OsS2b and potato AGPase heterotetramer (StLSStSS). Moreover, the yeast-two-hybrid results on OsL1OsS1, which resemble StLSStSS, suggest a differential protein assembly for OsL2OsS2b. Thus, the regulatory and catalytic mechanisms for plastidial AGPases (OsL1OsS1) could be different in rice culm and developing endosperm compared to those of OsL2OsS2b, which are predominantly found in rice endosperm.