Sandbox Reserved 1697

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This Sandbox is Reserved from 10/01/2021 through 01/01//2022 for use in Biochemistry taught by Bonnie Hall at Grand View University, Des Moines, USA. This reservation includes Sandbox Reserved 1690 through Sandbox Reserved 1699.

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7KIR

spinqualitylabelsall models Inositol plyphosphate 1-phosphatase 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 Sandbox 1677. 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 The function of 7KIR is dephosphorylating inositol, used in inositol signaling, the substrate of the enzyme is IP3 and the product is IP2. The amino acids of the protein hold onto the magnesium metal ions that then hold onto the water molecule, this allows for it to take off a phosphate. Biological relevance and broader implications The protein 7KIR is a protype member of a family of enzymes involved in dephosphorylation IP3. The two metal ions, Magnesium and Lithium, are particularly important in activation and inhibition of inositol signaling. Since these enzymes are seen in many different organisms, with slight mutations in the motif of the enzyme without change in function, understanding the mechanics of enzyme inhibition in this metabolic pathway would allow a better understanding of metabolic pathways. Important amino acids In this protein the amino acids do not interact with the substrate itself, instead they interact with the metal ions. When magnesium is present, and the protein therefore activated, the amino acids will hold onto the magnesium ions. These magnesium ions that interact with the inositol and water so that it can dephosphorylate the substrate. The motif of enzymes in this family is DPIDXT. In this particular protein the motif is D54, E80, E79, D153, and D317. There are some mutations in the enzyme but the overall function of the protein is still the same. Structural highlights This protein is a mutation of 1INP, it has thirteen structural elements. The amino acids in the bind to the substrate all participate in hydrogen bonding to the substrate and ligand. The structure is 77% helix and 23% beta sheet, the betta sheets allow for twisting of the molecule so that the ligand better fits within the enzyme. The helices allow for hydrogen bonding throughout to stabilize the structure with assistance from metal ions; specifically magnesium ions. There is no quaternary structures in the protein but several tertiary structures that play an important role in the structure of the protein and therefore its function. There are many covalent bonds due to hydrophobic and nonpolar amino acids that form the structure. The amino acids involved with the catalytic amino acids are mostly polar, the magnesium ions assist in pulling the enzyme into shape that allow for it to be in the proper shape so that it can dephosphorylate the inositol When the lithium ions interact with the enzyme a shape change occurs that will not allow for the magnesium ions to attach to the enzyme, and therefore the water molecules. Other important features The ligand of the protein is known as D-MYO-INOSITOL-1,4-BISPHOSPHATE, with a PDB ID of 2IP. The cyclic structure of the ligand could possibly assist with binding the substrate, the hydrogen bonding with various amino acids allows for many interactions with the enzyme. 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.