Sandbox Reserved 1559

This Sandbox is Reserved from Aug 26 through Dec 12, 2019 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 1556 through Sandbox Reserved 1575.

To get started: Click the edit this page tab at the top. 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

Overview

spinqualitylabelsall models Caption for this structure 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(s) and Biological Relevance Lignostilbene-α,β-dioxygenase A (LsdA) from the bacterium Sphingomonas paucimobilis TMY1009 is a nonheme iron oxygenase that catalyzes the cleavage of lignostilbene, a compound arising in lignin transformation, to two vanillin molecules. LsdA has greatest substrate specificity for lignostilbene. The substrate's 4-hudryoxy moiety is required for catalysis. Phenylazophenol inhibits the cleavage of lignostilbene by LsdA. The breaking down of lignin is essential to the sustainable biorefining of lignocellulose. It is of great relevance to transforming lignocellulose to biofuels. Broader Implications Lignin represents 30% of the lignocellulose biomass. It consists of different aromatic building blocks, phenylpropanoids, which are extremely useful. Normally aromatic compounds are extracted from petroleum and are used to manufacture drugs, paint, plastics, etc. Therefore the potential of lignin is very high. Lignin is the most abundant polymer in nature other than cellulose and chitin, and it is the only one that contains such a large number of aromatic compounds. Structural highlights and structure-function relationships The Catalytic Triad of the NSL ligand consists of Phenylalanine59, Tyrosine101, and Lysine134. The flat surface of the B-sheet is pushing the amino acids up, making it possible for the catalytic triad Phe59, Tyr101, and Lys134 to create interactions with the ligand. The tertiary structure creates a binding pocket of amino acids that are important to the active site. His282 provides pi-stacking, Phe305 provides Hydrophobic contacts, and Tyr101 provides Hydrogen bonding. The tertiary structure also allows the NSL ligand to interact using its 4-hydroxy with the catalytic triad. Energy Transformation 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.