Sandbox Reserved 1759

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This Sandbox is Reserved from November 4, 2022 through January 1, 2023 for use in the course CHEM 351 Biochemistry taught by Bonnie Hall at the Grand View University, Des Moines, USA. This reservation includes Sandbox Reserved 1755 through Sandbox Reserved 1764.

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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. The MVA3,5-bisphosphate decarboxylase enzyme was observed in Thermoplasma-type MVA pathway, specifically as a catalytic enzyme in the MBD reaction. The basic function of MVA3,5-bisphosphate decarboxylase 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. MVA 3,5-bisphosphate decarboxylase 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. The first domain contains 9 alpha helix and 15 beta sheets. The second domain contains 9 alpha helix and 15 beta sheets. In the first domain, the amino acid Arg148 that hydrogen bonds to the OLA ligand is contained within a beta sheet.