Official Project Description
Atomistic insights into AAA+ protein superfamily ATPases Associated with diverse cellular Activities (AAA+) comprise a superfamily of proteins that perform a large variety of functions essential to cell physiology, including control of protein homeostasis, DNA replication, recombination, chromatin remodeling, ribosomal RNA processing, molecular targeting, organelle biogenesis, and membrane fusion.
Members of this superfamily are defined by the presence of what is termed the AAA+ domain containing the canonical Walker A and B motifs required for ATP binding and hydrolysis.
Typically, genomes encode approximately ten to several hundred AAA+ family members, each of which is thought to be adapted to specific functional niches that necessitate precise mechanisms of substrate recognition and processing.
The striking adaptive radiation of AAA+ proteins to operate in diverse settings illustrates the versatile utility of the AAA+ domain.
AAA+ proteins typically form hexameric complexes and act as motors to remodel other proteins, DNA/RNA, or multicomponent complexes.
Indeed, many chaperones and ATP-dependent proteases are or have subunits that belong to this superfamily.
Rubisco activase (Rca) belongs to the AAA+ superfamily of proteins and it hydrolyzes ATP to ADP.
The complementarity of nucleotide-binding sites between AAA+ interfaces, the mechanism of ATP hydrolysis and the conformational changes activating or deactivating their ATP-binding pocket ensure a functional cycle that creates mechanical force to promote remodeling of substrates.
In this study, we will investigated the ADP/ATP and Mg2+ ion binding mechanism in Rca monomer and homodimers using extensive longtime scale simulations.
We will also try to find the binding pathway for ADP and ATP.
Simulations will also helps to predicts the crucial residues that involved in this binding process.