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Function of your Protein
The specific function of my protein is that it is an enzyme that comes from bacteria called Bacillus cereus. Its main function is to catalyze the chemical reaction by turning UDP-glucose into UDP- galactose in sugar-containing metabolites. It does this by flipping the chiral center. The PBD of this protein in 6ZLK and it contains 3 ligands. The 3 ligands are UGB, NAD, and UGA. I am focussing on is UGB.
Biological relevance and broader implications
In the article that was assigned to me, they are studying the double nature of the enzymatic mechanism. Specifically at the active site and looking at the flexibility required for rotation. This is relevant because it helps us understand how drugs work on the liver and how hormones affect the liver. Understanding this protein can help us understand how its hydrophilic tendencies can impact drug secretion. This protein contains a few sugar rings in its metabolic pathway. The process creates sugar products.
Important amino acids
Structural highlights
Our protein comes from the Bacillus cereus HuA2-4 organism. It includes the Epimerase domain. Our protein has a fair amount of secondary structures. This tertiary structure contains many hydrophobic interactions. There are 3 major ligand binding sites.: UGA, NAD, and UGB. This means that the amino acids at the binding sites have nonpolar R groups cluster together, on the inside of the protein. This leaves the hydrophilic amino acids on the outside of the structure.
The hydrophobic amino acids include THR, ILE, ALA, and PHE. This protein contains a few sugar rings in its metabolic pathway. The process creates sugar products. This enzyme creates a cavity where the sugar group binds and modifies itself. It has one Ramachandran Outlier. the total structure Weight is 153.40 kDa.The way that the protein is folded denotes that it might also be a quaternary structure.
Other important features
The enzyme prevents decarboxylation by keeping the CO2 on the structure. You can see this in scheme 1 where it breaks the double O bond on Carbon 4 and makes it alcohol and keeps the CO2 on the sugar structure. Another structural mechanism characteristic is that this protein has a lot of stacking. Hydrogen bond stacking benefits this protein by making it more structurally sound by helping the protein regulate electronegativity. You can see this on our protein in figure 2.A the block dotted lines are representing the hydrogen bonds in the structure. Our protein also consists of many Rossman folds. This is a super secondary structure. It is composed of alternating alpha and beta sheets. The first Rossman fold in a series is the one in contact with the nucleotide. In our protein, our nucleotide is the NAD. It contains a Rossman fold that had 7 𝛃- strands and 6 𝜶-helices. The Rossman folds help stabilize the binding in the protein, which helps the catalytic triad have more efficient binding. Figure 1 also shows that the crevice between the 2 domains encloses the active site. The crevice also denotes the hydrophobic interactions within the protein's 2 polypeptide faces. Hydrophobic interactions mean that the amino acids that have nonpolar r groups cluster together, on the inside of the protein. This leaves the hydrophilic amino acids on the outside of the structure. I saw a perfect example of this in figure 2. A, and 2.D. the protein we are studying contains F,Y, and L. Our protein also contains an enzyme-substrate complex. This is when an enzyme binds to the substrate and forms a complex. The result of the complex-forming causes the decrease in activation energy of the reaction and causes other ions and chemical groups to form covalent bonds creating additional steps in the process. This is shown in our protein in figure 7. In the presence of UDP-Glc, the enzyme closes over the substrate changing the position compared to the UDP- bound enzyme.
This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
