Team:ITESM-CEM/Oxoacyl

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     <td colspan="3" rowspan="3" align="left" valign="top"><ul>
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       <sub><a href="https://2014.igem.org/Team:ITESM-CEM/Modeling" style="color: #FFF;">Modeling Proteins</a></sub>
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       <sub><a href="https://2014.igem.org/Team:ITESM-CEM/Modeling">Modeling Proteins</a></sub>
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       <sub><a href="https://2014.igem.org/Team:ITESM-CEM/CholesterolOxidase" style="color: #FFF;">Cholesterol Oxidase</a></sub>
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       <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>  
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       <sub><a href="https://2014.igem.org/Team:ITESM-CEM/Cholesterol" style="color: #FFF;">7-Dehydratase</a></sub>
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       <sub><a href="https://2014.igem.org/Team:ITESM-CEM/Cholesterol">7-Dehydratase</a></sub>
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      <sub><a href="https://2014.igem.org/Team:ITESM-CEM/EnzymaticKinectics">Enzymatic Kinetics</a></sub>
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     <td><img src="images/spacer.gif" width="1" height="1" alt=""></td>
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<h2>Oxoacyl Reductase</h2>
<h2>Oxoacyl Reductase</h2>
    
    
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<p>The theoretical dehydratase has 602 aminoacids. The predicted secondary structure is the following.
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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>
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The theoretical dehydratase has 602 aminoacids. The predicted secondary structure is the following.The theoretical dehydratase has 602 aminoacids. The predicted secondary structure is the following.The theoretical dehydratase has 602 aminoacids. The predicted secondary structure is the following.The theoretical dehydratase has 602 aminoacids. The predicted secondary structure is the following.The theoretical dehydratase has 602 aminoacids. The predicted secondary structure is the following.The theoretical dehydratase has 602 aminoacids. The predicted secondary structure is the following.The theoretical dehydratase has 602 aminoacids. The predicted secondary structure is the following.The theoretical dehydratase has 602 aminoacids. The predicted secondary structure is the following.The theoretical dehydratase has 602 aminoacids. The predicted secondary structure is the following.The theoretical dehydratase has 602 aminoacids. The predicted secondary structure is the following.The theoretical dehydratase has 602 aminoacids. The predicted secondary structure is the following.The theoretical dehydratase has 602 aminoacids. The predicted secondary structure is the following.The theoretical dehydratase has 602 aminoacids. The predicted secondary structure is the following.
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<img src="https://static.igem.org/mediawiki/2014/0/08/Imagenes_enzimas_modelado-4.jpg" align="left" width="590" height="403" hspace="20"> </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>  
      
      
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<br><br><br>
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<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>
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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>
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<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.
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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.
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</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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Latest revision as of 15:48, 14 October 2014

TEC-CEM | Modeling

ITESM-CEM | Enzy7-K me

Modeling 3325
 

Oxoacyl Reductase

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.


The theoretical dehydratase has 602 aminoacids. The predicted secondary structure is the following.


Physicochemical Characteristics

Table 1. Oxoacyl reductase physicochemical characteristics obtained from XTalPred-RF


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 3D structure are fairly similar. An interesting piece of information is that most of the registered Oxoacetil reductases work in homo 4-mers.



Figure 1. Structural alignment between Oxoacyl reductase from Rhodococcus jostii (blue) and the 3-oxoacyl-acyl carrier protein reductase from Staphylococcus aureus (red).


Figure 2.3D configuration comparison between the between Oxoacyl reductase from Rhodococcus jostii (left) and the 3-oxoacyl-acyl carrier protein reductase from Staphylococcus aureus (right).




 

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