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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 and it contains 3 ligands. The 3 ligands are UGB, NAD, and UGA. I am focusing on UGB. The substrate in our Protein is NAD+. In our protein, the substrate and product bound enzymes 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. Even though changing Glucose into Galactose is a reaction near equilibrium and can be reserved because there isn't a big energy change, Studying this enzyme can help with biocatalysis. Biocatalysis is defined as the use of natural substances that include enzymes from biological sources or whole cells to speed up chemical reactions. In doing research on this enzyme-substrate complex it can help with improving the knowledge base of how catalysis impact reactions that include the production of alcohols from fermentation and cheese by the breakdown of proteins. The same types of enzymes that can be used in the food process, can be used in drug uptake. Enzymes as drugs have features that separate them from all other types of drugs. Enzymes often bind and act on their targets with great affinity and specificity. By looking at how a simple swing and flip of a pro-chiral 4-keto-hexose can change the molecule altogether and can change the whole structure and function of the protein. Second, enzymes are catalytic and convert multiple target molecules to the desired products. By adding different substrates and changing the formation of the structure, that can create many different products as we see in figure 6.

Important amino acids

Focussing on , Some important Amino acids would be , Threonine(126), and Tyrosine(149) I found in the article that Lysine(153) is part of the triade also. They are in my enzyme.THR and TYR are Amphipathic. This means they have both hydrophilic and hydrophobic parts. Serine, Threonine, and Tyrosine are Polar. Polar hydrophilic amino acids are important in UGB ligand binding to the substrate. The interactions play an important role in "molecular recognition". Different polarity means that there is a different charge distribution among the amino acids. This becomes important for locating or identifying the accessible area to the substrate. I found that the rings on the end have a lot to do with binding. The key Amino acids for binding from the website and the article are Pro, Gly, and Arg. which you can also see in figure 2D. When I used the RCSB website I saw that the sugar rings were intertwined. These key amino acids are important because they participate in hydrogen bonding. The 4th carbon engages the residues in the triad. The 2nd carbon with the OH attached to it and the 3rd carbon with the OH is hydrogen-bonded to ARG-185 and PRO-85. The 5th carbon on the carboxylate interacts with the THr-126, Ser-127, and the Ser-128. With the hydrogen bonding happening at the site, the negative charges are what drive the strained backbone. The sugar cavity has 3 water in it and they overlap the 3’-OH,4’-OH, and 5’- carbonate groups.

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. 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. 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 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. 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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