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This is a Proteopedia created to explain the function and structure of Mevalonate 3,5-bisphosphate decarboxylase

Function of your protein

is a protein that originates from members of the order Thermoplasmatales, however in this article specifically the Mevalonate 3,5-bisphosphate being studied originated from the species Picrophilus Torridus. The purpose of this protein is to catalyze an elimination reaction in order to remove the 3-phosphate group from mevalonate 3,5-biphosphate and further goes on to decarboxylate the substrate produced thereby removing carboxyl groups from the acidic substrate.

Biological relevance and broader implications

Important amino acids

The article only really talks about how the ligand, like a fatty acid, lacks an ATP binding site. It also talks about the necessity of the ligand being amphipathic as there are hydrophilic and hydrophobic charges found in the binding site.

Structural highlights

The protein is a dimer that contains per linked molecule. The ARG 148 forms hydrogen bonds that allow it to pair with Oleic Acid, the protein’s ligand. Protein also requires H2O to be present in order to bind its . I found it really interesting that the protein only actually attaches to the ligand via small interaction between ARG 148 and water molecules.

This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.