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Mevalonate 3,5-Bisphosphate Decarboxylase Structure

spinqualitylabelsall models Caption for this structure Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D 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. Ligand of interest, Oleic Acid (OLA) Important amino acids Ligand OLA is hydrogen bonded to Arg128. 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 structure. Each subunit contains 9 alpha helix and 15 beta sheets. In the first subunit, the amino acid Arg148 that hydrogen bonds to the OLA ligand is contained within a beta sheet. The alpha helixes and beta sheets loop and fold to form a 3D globular protein. The space filling model helps to highlight the globular nature of the protein and