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Structure

The AAT D22T mutant consists of two chains that are made up of alpha-helices. Unlike normal aspartate aminotransferase, it does not contain any beta-sheets. the D222T variant has 7438 non-hydrogen atoms and 6608 macromolecules with no bound ligands. It has a length of 414 amino acids. It also has a wavelength of 0.97856 Å. When looking at the homodimer structure, the two distinctive chains can be seen (chain A and chain B). In , multiple conformations can be seen; however, the crystal packing restrains its small domain and its movement (NLM). Chain B is not restrained like chain A, making its small domain more mobile. The hydrogen-bonding networks differ between the chains, as well as the different mutants. This enzyme is commonly found in E. coli that is in sus scrofa or swine, meaning wild boar, hog, or pig.

Function

Amino acids are the foundation of proteins and are also the building blocks of life. Understanding the residues of these amino acids and their roles is one of the most challenging aspects of modern biology. The synthesis and breakdown of these building blocks is called amino acid metabolism. The enzyme aspartate aminotransferase cytoplasmic D222T mutation or AAT D222T mutant plays a very interesting part in that process. Putting the name into layman’s terms, AAT is the enzyme, while D222T is the actual single mutation of that enzyme. This mutant is in close relation to H143, T139, and H189 mutants. It is classified as a transferase, which means they catalyze the transfer of specific functional groups from one molecule to another.

Relevance

This enzyme is commonly found in E. coli that is in sus scrofa or swine, meaning wild boar, hog, or pig. Getting into the taxonomy of sus scrofa is important. Classified as even-toed ungulates, they fall under the Animalia kingdom, Mammalia class, and the Chordata phylum. Originating from North Africa and Eurasia, the wild swine has the widest-ranging mammal in the world. They inhabit a tremendous array of habitats all over the planet; so much so that they are considered an invasive species. On record, there are about 599 specimens and 4 subspecies (boldsystems). These subspecies include Sus scrofa cristatus, Sus scrofa domesticus, Sus scrofa scrofa, and Sus scrofa taivanus. These creatures have a long history of association with humans, which has led to them becoming the most widespread suiform. Due to this expansion, it has been seen that there is a massive change in gene expression and gene regulation during the adaptation to these new habitats (biomedcentral). Their divergence around 1.5 million years ago, as well as human-mediated dispersal, has led to the current results in their gene flow. It also resulted in very different minor allele frequencies at millions of genomic locations (biomedcentral). It is not normally recognized that due to domestication and selection by humans, the phenotypic variation of sus scrofa is incredibly large. Due to this, as time went on, this species has seen genes rapidly evolve and involve themselves in host defense, immunity, and sensory perception. Due to the great changes in gene regulation within Sus scrofa, this likely resulted in mutations such as the D222T mutant. The gene in question that affects the amino acid metabolism and produces aspartate aminotransferase within the sus scrofa population is called Glutamate Oxaloacetate Transaminase 1 (GOT1). GOT1 is conserved and present in many other species including Homo sapiens. In sus scrofa, the gene is typically expressed in the heart and a few other tissues. Not only does it play a role in amino acid metabolism, but it is also present for the urea and tricarboxylic cycles, as well as a slew of other processes. The GOT1 gene regulates general cell metabolism through the usage of carbohydrates and amino acids to meet nutrient requirements in the body. Part of that regulation, as stated before, includes amino acid metabolism through informational coding of aspartate aminotransferase.

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