Sandbox Reserved 1061

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

Structure of Mycobacterium Tuberculosis NrdH

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. This page is for Bryant Dawson and Kate Burke hehehe Overview Mycobacterium tuberculosis NrdH is a small glutaredoxin-like protein involved in the electron transport chain that eventually leads to ribonucleotide reduction. Background Mycobacterium tuberculosis resides in the lungs of a host and upon becoming active, results in symptoms such as chest pains, weakness, and intense coughing. Left untreated and unmanaged, TB can lead to death (1.5 million in 2013). The disease has a high co-morbidity with HIV/AIDS due to its immunocompromising tendencies. Tuberculosis is one of the most heavily studied diseases today. With over 9 million infections worldwide per year, the necessity for antimicrobial agents to combat emerging multi-drug resistant strands is imperative. Structure The structure of M. tuberculosis as determined by x-ray crystallography has 79 residues in a single polypeptide chain. NrdH Chrystal Structure. The active site (shown in green) is dominated by a disulphide bond between Cys-11 and Cys-14, which serves as the site of reduction by Theirodoxin reductase. Many Theirodoxin-like proteins have a similar active site region, denoted as the Theirodoxin fold, which occurs directly before the disulfide bond. The residues in this region, denoted by letters CVQC, are the most highly conserved of all areas of the protein across multiple species. Exactly how this structure relates to function is somewhat debated. A Threonine-6 reside directly across the theirodoxin fold from the disulphide bond has been suggested to adopt two different conformations which differentially affect the redox abilities of the Protein. In the A conformation, the alcohol of the threonine side chain points towards the disulfide bond, engaging an ionic interaction between the two that prevents the Therodoxin Reductase from binding. Alternatively, in the B conformation, the alcohol points in the opposite direction, allowing sufficient space for the ligand to bind and reduction to occur. File:Disulfide bond with ligand.png Function TextToBeDisplayed 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.