Sandbox Reserved 1065

This Sandbox is Reserved from 02/09/2015, through 05/31/2016 for use in the course "CH462: Biochemistry 2" taught by Geoffrey C. Hoops at the Butler University. This reservation includes Sandbox Reserved 1051 through Sandbox Reserved 1080.

To get started: Click the edit this page tab at the top. Save the page after each step, then edit it again. Click the 3D button (when editing, above the wikitext box) to insert Jmol. 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

Your Heading Here (maybe something like 'Structure')

spinqualitylabelsall models Very Long Chain Fatty Acyl CoA Synthetase (FadD13) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D General mechanism for the activation of fatty acids FadD13 first activates the fatty acid through a reaction with ATP to form an acyl adenylate intermediate and release pyrophosphate. Following a conformational change of the enzyme, coenzyme A is able to bind and reaction with the acyl adenylate intermediate forming the acyl CoA product (Figure 1). active site (to be copied over) Mutational studies showed that high conserved residue in the C-terminal region, Lysine 487, resulted in a 95% loss of function of FadD13 and is thought to be involved in the orientation of the substrates to form the adenylate intermediate. Additionally, Serine 404 was hypothesized to be involved in the binding of Coenzyme A which may only occur once this region incurs a 140 degree rotational change. Function This is the Arginie-rich lid loop. This is the linker. FadD13 has three different regions: The N-terminal region (1-395) is in blue, the C-terminal region (402-403) is in red, and the six amino acid linker is in tan (citation for original paper). The adenine of ATP is bound to a group of six amino acids (300-305) that is structurally identically to other acyl-CoA synthetases (Citation for original paper). citation 1 citation 2 Citation 3 Structural highlights 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.