Glycine Mutant of Glutathione Peroxidase 1</scene>' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />
| This Sandbox is Reserved from 4/28/214, through 6/28/214 for use in the course "Proteins" taught by Drew Barber at the Univeristy of Vermont. This reservation includes Sandbox Reserved 186 through Sandbox Reserved 189.
|
To get started:
- Click the edit this page tab at the top. Save the page after each step, then edit it again.
- Click the 3D button (when editing, above the wikitext box) to insert Jmol.
- show the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page.
- Add a description of your scene. Use the buttons above the wikitext box for bold, italics, links, headlines, etc.
More help: Help:Editing
|
Glutathione Peroxidase 1
Overview
Glutathione peroxidase 1 (GPx-1) is a tetramer (23 kDa per monomer) with two units composed of dimers. GPx-1 is the most abundant member of the Glutathione peroxidase family. It is found in all cells and is located in the cytosolic and mitochondrial compartments (1). GPx-1 is a crucial anti-oxidant enzyme that catalyzes the conversion of hydrogen peroxide into water (2). Interestingly GPx-1 contains the rare amino acid selenocysteine which acts as the peroxidatic residue (2). The overall reaction that GPx-1 catalyzes is H2O2 + 2Glutathione (GSH) -> 2H20 + GS-SG (Figure 1). In addition to hydrogen peroxide GPx-1 can reduce other soluble hydroperoxides including lipid hydroperoxides (3). Because of its role in regulating the intracellular concentration of reactive oxygen species, GPx-1 has been found to play a role in numerous processes including cell proliferation, apoptosis, and inflammation (1). Furthermore deficiencies in GPx-1 has been linked to the development of cancers, neurodegenerative diseases, and heart disease (4).
Secondary Structure and the Thioredoxin Like Fold
GPx-1 consists of nine β-strand nine α-helices with four of the helices being of the 310 form (Figure 2). Interestingly two of the β-strands form a parallel β-sheet (Figure 3)
. The classic thioredoxin fold consists of a four stranded β-sheet that is surrounded by three α-helices (5). However the thioredoxin fold is commonly subject to the insertion of additional secondary structural elements between the second β-strand and the second α-helices (6). This is seen in GPx-1 as there is an addition of an α-helix and a β-strand between the second β-strand and the second α-helices (6). A similar insertion is found in peroxiredoxins, a different family of proteins which also catalyze the reduction of hydroperoxides (6).
Relevance
Structural highlights
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.
</StructureSection>
References
