Sandbox Reserved 1759

Function of your protein

The protein of interest is the enzyme mevalonate 3,5-bisphosphate decarboxylase (MBD). The MBD enzyme was observed in Thermoplasma-type MVA pathway, specifically as a catalytic enzyme in the MBD reaction. The function of MBD is to catalyze the removal of the phosphate group from the 3rd carbon of mevalonate 3,5-bisphosphate (MVA3,5BP). The enzyme also accompanies the decarboxylation of the substrate. MBD acts upon MVA3,5BP to produce isopentnyl phosphate (IP), PO4, and CO2 in the MBD reaction.

, Oleic Acid ()

Biological relevance and broader implications

Important amino acids

Ligand OLA is hydrogen bonded to . OLA is also hydrogen bonded to a water molecule which is hydrogen bonded to Arg128.

Structural highlights

The Protein is composed of alpha helix, beta sheet, and other structures. The protein consists of two major domains with what appears to be a 60% alpha helixes (pink) and 40% beta sheets (yellow) when viewing the . The two subunits are homodimers, containing 9 alpha helix and 15 beta sheets each. In the first subunit, the amino acid Arg148 that hydrogen bonds to the OLA ligand, which is contained within a beta sheet. The alpha helixes and beta sheets loop and fold to form a . The model helps to highlight the globular nature of the protein.