Choline Oxidase: Difference between revisions

                  The RasMol 2.6.5.1 was used to model choline oxidase and the seven evolutionarily preserved amino acids. For this to work, the model of choline oxidase was needed from the protein databank. This file was found, and saved, in the same folder as the RasMol program, as ‘2JBV.spt.’ It was opened in RasMol and the background was changed to white. One subunit of choline oxidase was restricted. The remaining plain subunit was given a backbone of 300 RasMol units and the wireframe of the amino acids residues was turned off. Each RasMol unit is 1/250 of an angstrom. The seven preserved amino acids and the flavin group were space filled with 275 RasMol units and wireframed with 225. The preserved residues were also highlighted in cyan. The three preserved residues closest to the FAD ligand were then changed to a blue color. Monitor lines were drawn between these three residues and the FAD prosthetic group, which was left in the original CPK color (see Figure 2). The monitor lines were colored white and spacefilled with 275 RasMol units. Beta sheets were colored yellow and highlighted the secondary structure of the molecule. Hydrogen bonds and more monitor lines were also added and colored white to support the model.