Sandbox Reserved 1758

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.

To get started: Click the edit this page tab at the top. Click on Show preview and then Save the page after each step, then edit it again. show the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page. Add a description of your scene. Use the buttons above the wikitext box for bold, italics, links, headlines, etc. More help: Help:Editing

Mevalonate 3,5-biphosphate decarboxylase

spinqualitylabelsall models 7T71 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D This is a default text for your page '. Click above on edit this page' to modify. Be careful with the < and > signs. You may include any references to papers as in: the use of JSmol in Proteopedia or to the article describing Jmol to the rescue. 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 ATP-dependent phosphorylation of the 3-hydroxy group of substrates. The protein binds to an amphipathic fatty acid, Oleic Acid. This is the ligand represented in the structure however the authors noted that archaea do not tend to synthesize fatty acids. The authors determined that GGPP or related compounds are possible physiological ligands. Biological relevance and broader implications The enzyme catalyzes the elimination of the 3-phosphate group from mevalonate 3,5-biphosphate as well as concomitant decarboxylation of the substrate.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 catalytic dyad 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 ligand that is bound to it. This is a sample scene created with SAT to color by Group, and another to make a transparent representation of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.