RESEARCH: AAA-PROTEIN-SUPERFAMILY
FOLDING PROJECT #19325 PROFILE

This project explores how Rubisco activase (Rca), a protein important for plant growth, uses energy from ATP to change shape and do its job. Researchers will use computer simulations to understand how Rca binds to ATP and ADP (chemicals related to energy) and figure out which parts of the protein are most important for this process.

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.

AAA+ protein superfamily

A superfamily of proteins involved in diverse cellular functions.

AAA+ proteins are a large group of proteins found in all living organisms. They play important roles in many cellular processes, such as DNA replication, protein folding, and cell division. AAA+ proteins are named after their ATPase activity and conserved domains.

ATPases

Enzymes that hydrolyze ATP to ADP, releasing energy.

ATPases are a type of enzyme that breaks down a molecule called ATP (adenosine triphosphate). ATP is the primary energy source for cells. When ATP is broken down by an ATPase, energy is released that can be used to power various cellular processes.

AAA+ domain

A protein domain containing Walker A and B motifs involved in ATP binding and hydrolysis.

The AAA+ domain is a region within proteins that is responsible for binding and breaking down ATP. This process releases energy that the protein can use to perform its functions.

ATP

Adenosine triphosphate

ATP is the primary energy currency of cells. It's a molecule that stores energy and releases it when needed for various cellular processes.

ADP

Adenosine diphosphate

ADP is a molecule produced when ATP loses one phosphate group. It's often involved in energy-related processes.

Mg2+

Magnesium ion

A positively charged magnesium atom that plays a role in many enzymatic reactions and cellular processes.