Sandbox Reserved 497

This Sandbox is Reserved from 13/03/2012, through 01/06/2012 for use in the course "Proteins and Molecular Mechanisms" taught by Robert B. Rose at the North Carolina State University, Raleigh, NC USA. This reservation includes Sandbox Reserved 451 through Sandbox Reserved 500.

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 For more help, look at this link: http://www.proteopedia.org/wiki/index.php/Help:Getting_Started_in_Proteopedia Dimethylsulfoniopropionate-Dependent Demethylase A (DmdA))Dimethylsulfoniopropionate-Dependent Demethylase A (DmdA)) spinqualitylabelsall models Dimethylsulfoniopropionate-Dependent Demethylase A (DmdA), 3TFH Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image IntroductionIntroduction StructureStructure The structure of DmdA was recently solved through X-Ray Diffraction. The structure contains 369 amino acids folded into four domains and containing two ligands. Mechanism of ActionMechanism of Action The specific mechanism of DmdA is still being investigated. However, a mechanism was recently proposed Possible ApplicationsPossible Applications ReferencesReferences Image from the RCSB PDB (www.pdb.org) of PDB ID 3TFH (Schuller, D.J., Reisch, C.R., Moran, M.A., Whitman, W.B., Lanzilotta, W.N. (2012) Structures of dimethylsulfoniopropinate-dependent demethylase from the marine organism pelagabacter ubique. Protein Sci. 21: 289-298.