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You may include any references to papers as in: the use of JSmol in Proteopedia ^[1] or to the article describing Jmol ^[2] to the rescue.

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. The substrate in our Protein is NAD+. In our protein, the substrate and product bound enzymes to co-exist which creates an equilibrium structure. The product is UDP-GlcA and it reacts with the substrate NAD+ which creates the product of UDP- GalA.

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 the industrial applications of how enzymes work. Enzymes are used in the food industry quite often, They are used to manufacture dairy, meat, and bakery items. Understanding this protein can help us understand how its hydrophilic tendencies can impact the products it creates. This protein contains a few sugar rings in its metabolic pathway. The process creates sugar products. Studying Enzyme kinetics is important because enzymes are important to life. Understanding This information provides information about many diverse reactions, which helps us predict the metabolism of all living things. Biocatalysis is defined as the use of natural substances that include enzymes from biological sources or whole cells to speed up chemical reactions

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.

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