Team:ITESM-CEM/Oxoacyl
From 2014.igem.org
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- | <sub><a href="https://2014.igem.org/Team:ITESM-CEM/Modeling | + | <sub><a href="https://2014.igem.org/Team:ITESM-CEM/Modeling">Modeling Proteins</a></sub> |
- | <sub><a href="https://2014.igem.org/Team:ITESM-CEM/CholesterolOxidase | + | <sub><a href="https://2014.igem.org/Team:ITESM-CEM/CholesterolOxidase">Cholesterol Oxidase</a></sub> |
<sub><a href="https://2014.igem.org/Team:ITESM-CEM/Oxoacyl" style="color: #FFF;">Oxoacyl Reductase</a></sub> | <sub><a href="https://2014.igem.org/Team:ITESM-CEM/Oxoacyl" style="color: #FFF;">Oxoacyl Reductase</a></sub> | ||
- | <sub><a href="https://2014.igem.org/Team:ITESM-CEM/Cholesterol | + | <sub><a href="https://2014.igem.org/Team:ITESM-CEM/Cholesterol">7-Dehydratase</a></sub> |
- | <sub><a href="https://2014.igem.org/Team:ITESM-CEM/EnzymaticKinectics | + | <sub><a href="https://2014.igem.org/Team:ITESM-CEM/EnzymaticKinectics">Enzymatic Kinetics</a></sub> |
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<p style="text-align: justify; text-justify: inter-word;"> This tridimensional model was obtained with the I-TASSER software. It has a -0.70 C-score which makes it, out of the 5 predicted models, the more plausible to be the actual tridimensional conformation of the protein. </p> | <p style="text-align: justify; text-justify: inter-word;"> This tridimensional model was obtained with the I-TASSER software. It has a -0.70 C-score which makes it, out of the 5 predicted models, the more plausible to be the actual tridimensional conformation of the protein. </p> | ||
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+ | <p class="centeredImage"><img src="https://static.igem.org/mediawiki/2014/8/8c/Oxoacyl1.jpg" width="390" height="203" hspace="20"></p><br> | ||
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<p style="text-align: justify; text-justify: inter-word;">The theoretical dehydratase has 602 aminoacids. The predicted secondary structure is the following. </p> | <p style="text-align: justify; text-justify: inter-word;">The theoretical dehydratase has 602 aminoacids. The predicted secondary structure is the following. </p> | ||
- | <p><img src="https://static.igem.org/mediawiki/2014/0/08/Imagenes_enzimas_modelado-4.jpg | + | <p class="centeredImage"><img src="https://static.igem.org/mediawiki/2014/0/08/Imagenes_enzimas_modelado-4.jpg" width="520" height="333" hspace="20"></p><br> |
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<h2>Physicochemical Characteristics</h2> | <h2>Physicochemical Characteristics</h2> | ||
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+ | <p><pie>Table 1. Oxoacyl reductase physicochemical characteristics obtained from XTalPred-RF</p> | ||
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+ | <p class="centeredImage"><img src="https://static.igem.org/mediawiki/2014/0/05/Tabla_2.JPG"></p><br> | ||
<p style="text-align: justify; text-justify: inter-word;"> When a BLAST was performed several results were obtained which fulfilled a similarity of over 95%, all of them were registered and characterized Oxoacetil reductases from other organisms. | <p style="text-align: justify; text-justify: inter-word;"> When a BLAST was performed several results were obtained which fulfilled a similarity of over 95%, all of them were registered and characterized Oxoacetil reductases from other organisms. | ||
- | The structural comparison was made with a 3-oxoacyl-acyl carrier protein reductase from Staphylococcus aureus. As it can be observed in the figures bellow the | + | The structural comparison was made with a 3-oxoacyl-acyl carrier protein reductase from Staphylococcus aureus. As it can be observed in the figures bellow the 3D structure are fairly similar. An interesting piece of information is that most of the registered Oxoacetil reductases work in homo 4-mers. |
- | </p><br><br><br> | + | </p><br> |
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+ | <p class="centeredImage"><img src="https://static.igem.org/mediawiki/2014/c/c8/Oxoacyyl.jpg" width="390" height="203"></p><br> | ||
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+ | <p><pie><b>Figure 1.</b> Structural alignment between Oxoacyl reductase from Rhodococcus jostii (blue) and the 3-oxoacyl-acyl carrier protein reductase from Staphylococcus aureus (red).</p></pie> | ||
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+ | <p class="centeredImage"><img src="https://static.igem.org/mediawiki/2014/6/65/Oxoacyl2.jpg" width="390" height="203"></p><br> | ||
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+ | <p><pie><b>Figure 2.</b>3D configuration comparison between the between Oxoacyl reductase from Rhodococcus jostii (left) and the 3-oxoacyl-acyl carrier protein reductase from Staphylococcus aureus (right).</p></pie><br><br><br> | ||
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