Sandbox Reserved 1108

This Sandbox is Reserved from 25/11/2019, through 30/9/2020 for use in the course "Structural Biology" taught by Bruno Kieffer at the University of Strasbourg, ESBS. This reservation includes Sandbox Reserved 1091 through Sandbox Reserved 1115.

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

4iv6

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 4iv6 functions were not studied and only structural infos are disponible. Nevertheless we can consider datas from other E.C.1.3.8.1[1] which came from other organisms. Butyryl-CoA Dehydrogenase[2]. Primary and Secondary structure Isovaleryl-CoA dehydrogenase is the assembly of two asymmetric units each composed of two chains A and B linked by a ligand (Dihydroflavine-Adenine Dinucleotide also known as FADH2 ). Each of the two chains A and B are composed of 388 amino acids. An asymmetric unit is therefore composed of 776 amino acids and has a molecular weight of 86233.70 Da. The A chain is made up of 17 helices (involving 221 residues) and 14 beta-sheets (61 residues). Chain B is formed of 17 helices (involving 218 residues) and 14 beta-sheets (62 residues). Enzymatic reaction Enzyme accepted name: Short-chain acyl-CoA dehydrogenase Other names:Butanoyl-CoA dehydrogenase, Butyryl dehydrogenase, Short-chain acyl CoA dehydrogenase, Unsatured acyl-CoA reductase. Enzyme class: E.C.1.3.8.1[3] Substrate: A short-chain acyl CoA Prosthetic group: 1 electron-transfer flavoprotein such as FDA, for every Subunits Products: a short-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein Informed Pathways: Fatty acid degradation Other information: The enzyme from beef liver can accept acyl-chain lengths from 3 to 8 carbon atoms. From different organism the range can vary so we ignore if M.tuberculosis gets the same lengths resolution. The highest activity reported for beef liver enzyme was for substrates with 4 and 5 carbon acyl-chain lengths. 4IV6 as a research tool 4iv6 which belong to Mycobacterium tuberculosis was studied with other protein homolog. They were chosen to be studied as potential TB-Drugs target Studies have been made on homolog similarities aimed on their active site because with the knowledges of many homolog active site structure and how they work, we can design a inhibitor of those enzyme which can stop essential reaction and reduce or stop M.tuberculosis infection. This strategy is called an « Homolog-rescue strategy ». This strategy can be generalized for other drug target for other diseases. Structural highlights Biological unit Asymetrical unit :Light Grey:1st sub-unit, Light green:2nd sub-unit, Blue and red:FDA Secondary structure : Red: helix alpha, Blue:FDA, Yellow: Beta sheet Hydrophobic region : Green: FDA, Purple: Polar region, Light grey: Hydrophobic region