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 [1] or to the article describing Jmol [2] to the rescue.
Function of your protein
Our protein, L-rhamnose- α-1,4-D-glucuronate lyase (FoRham1), derived from the fungus Fusarium oxysporum, is a helpful tool for determining the structure and function of Gum Arabic (GA) to create potential agents to degrade GA more effectively. FoRham1, when bound to GA, will remove the Rha-caps from the nonreducing ends of GA. Enzymes that can react with glycosidic linkages of certain carbohydrates can be useful in determining the structure, function, and mechanism of the carbohydrates, giving scientists the tools to manipulate their physical properties for further application. Understanding the mechanism will give researchers more tools to understand how to degrade GA. Specifically, I focused on the mutant H105F, which has a PDB file of 7ESN.
Here, I have the protein using N->C coloring.
Biological relevance and broader implications
Gum Arabic (GA) is a representative protein of the family of arabinogalactan proteins (AGPs) and is produced in acacia trees in response to stress conditions, such as drought or wounds. GA has a variety of applications within the industrial world, including the food, cosmetic, and pharmaceutical industries, acting specifically as an emulsion stabilizer, emulsifier, and thickener in pharmaceutical settings.
Important amino acids
Amino Acids provide important interactions for binding. The His105 side chain forms a hydrogen bond with His85 side chain, providing stabilizing assistance. [3].
Amino Acid Residues form a hydrogen bond with the O-1 atom of Rha, suggesting these residues aid in the stabilization and elimination reactions.
Structural highlights
Secondary Structure: In this protein, there are around 30 anti-parallel beta sheets, two small hydrophobic alpha helices, and one alpha helix. The anti-parallel beta sheets provide further stabilization, through strong hydrogen bonding in the backbone, of the protein compared to parallel beta sheets. The hydrophobic alpha helices provide structure for the formation of the active site.
Other important features
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.
