Sandbox Reserved 1759

Function of your protein

The protein of interest is the enzyme . 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.

Biological relevance and broader implications

Important amino acids

The in the MBD enzyme is called and is located within subunit A. OLA is hydrogen bonded to .

Structural highlights

The MBD protein is composed of alpha helix, parallel and anti-parrallel beta sheet, and random coils. The protein consists of two major domains with a 60% alpha helixes (pink) and 40% beta sheets (yellow) when viewing the tertiary . The two subunits of the protein are homodimers, containing essentially identical alpha helixes and beta sheets between the two subunits, with intermolecular forces such as hydrogen bond connecting them. The alpha helixes and beta sheets loop and fold to form a structure. The model helps to highlight the globular nature of the protein. The two subunits are held together by non covalent.......Amphipathic.....In addition to the hydrogen bonding between OLA and Arg128, OLA is also hydrogen bonded to a water molecule which is hydrogen bonded to Arg128 as well

MBD is ATP-independent but evolves from the ATP-dependent , The MBD enzymes ligand binding site overlaps with the ATP binding site of its homologous enzyme, DMD.