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Function of your protein

Mevalonate 3,5-biphosphate decarboxylase is found in Picrophilus Torridus, a thermoacidophilic archaeon of the order Thermoplasmatales. The enzyme catalyzes the elimination of the 3-phosphate group from mevalonate3,5-biphosphate as well as concomitant decarboxylation of the substrate, GGPP.

Biological relevance and broader implications

Picrophilus Torridus undergoes Thermoplasma-type MVA (mevalonate). This is relevant because the journal is analyzing a distinction between a novel variant of the eukaryotic MVA pathway.

Important amino acids

The is composed of Asp 281 and Asp 309.

Structural highlights

Secondary Structure PtoMBD is a homodimer, chains A and B are two asymmetrical monomers that contain both alpha helices and beta sheets. The chains are nearly identical and contain 12 alpha helices and 12 beta sheets. The outer surface is framed by an antiparallel beta-sheet that is composed of β6, β4,β1, and β12 followed along with the β5 strand. Other antiparallel beta-sheets include the formation of β2, β3, β7, β8 and β9, β11, and β10 strands. These two beta-sheets alongside α1, α8, α9, α10, α11, and α12 helices form the floor of the enzyme as well as a large cleft of the substrate-binding sites. The upper domain of the site is formed of α2, α3, α4, α5, α6, and α7 helices and β5, β6, β4, β1, β12.There is a resemblance to homologous decarboxylases seen in the GHMP kinases superfamily. The PtoMBD homodimer has a calculated mass of 42,186 Da. My protein is important for saving the world, as can see by the amazing that is bound to it. 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.