Team:ITESM-CEM/CholesterolOxidase

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<p class="centeredImage"><img src="https://static.igem.org/mediawiki/2014/6/61/Colox1.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> <br><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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<p class="centeredImage"><img src="https://static.igem.org/mediawiki/2014/0/08/Imagenes_enzimas_modelado-4.jpg" width="625" height="226" hspace="20"></p>
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<p class="centeredImage"><img src="https://static.igem.org/mediawiki/2014/0/08/Imagenes_enzimas_modelado-4.jpg" width="625" height="426" hspace="20"></p>
<h2>Physicochemical Characteristics</h2>
<h2>Physicochemical Characteristics</h2>
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<p><pie><b>Table 1.</b> Cholesterol oxidase physicochemical characteristics obtained from XTalPred-RF.</pie></p>
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<p class="centeredImage"><img src="https://static.igem.org/mediawiki/2014/9/99/Tabla_colox.JPG" hspace="20"></p><br>
<p style="text-align: justify; text-justify: inter-word;"> The following pictures are the structural comparison between two different secuences of the cholesterol oxidase from Chromobacterium sp.<br>
<p style="text-align: justify; text-justify: inter-word;"> The following pictures are the structural comparison between two different secuences of the cholesterol oxidase from Chromobacterium sp.<br>
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Logically, the results showed a 100% similarity when a BLAST was performed. The only discrepancies found exist on the ends of the protein. Were in figure 4 it can be appreciated a red helix that belongs to the cholesterol oxidase expressed by the iGEM team ITESM.CEM. It is noteworthy that this enzyme works as a monomer. </p> <br><br><br>
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Logically, the results showed a 100% similarity when a BLAST was performed. The only discrepancies found exist on the ends of the protein. Were in figure 4 it can be appreciated a red helix that belongs to the cholesterol oxidase expressed by the iGEM team ITESM.CEM. It is noteworthy that this enzyme works as a monomer. </p> <br>
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<p class="centeredImage"><img src="https://static.igem.org/mediawiki/2014/3/3a/DEHIDRATASA_HIPOT%C3%89TICA-6.jpg" width="390" height="203" hspace="20"></p>
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<p><pie><b>Figure 1.</b> Structural alignment between two variations of the cholesterol oxidase from Chromobacterium sp. The one expressed by the team is highlighted in red, whereas the reference one is marked in blue. </pie></p><br>
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<p class="centeredImage"><img src="https://static.igem.org/mediawiki/2014/c/c5/Colox3.jpg" width="390" height="203" hspace="20"></p>
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<p><pie><b>Figure 2.</b>3D configuration comparison between two variations of the cholesterol oxidase from Chromobacterium sp. The one expressed by the team is left,  the reference one is on the right. </pie></p><br>
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Latest revision as of 15:06, 14 October 2014

TEC-CEM | Modeling

ITESM-CEM | Enzy7-K me

Modeling 3325
 

Cholesterol oxidase

This tridimensional model was obtained with the I-TASSER software. It has a - 1.34 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. Cholesterol oxidase physicochemical characteristics obtained from XTalPred-RF.


The following pictures are the structural comparison between two different secuences of the cholesterol oxidase from Chromobacterium sp.
Logically, the results showed a 100% similarity when a BLAST was performed. The only discrepancies found exist on the ends of the protein. Were in figure 4 it can be appreciated a red helix that belongs to the cholesterol oxidase expressed by the iGEM team ITESM.CEM. It is noteworthy that this enzyme works as a monomer.


Figure 1. Structural alignment between two variations of the cholesterol oxidase from Chromobacterium sp. The one expressed by the team is highlighted in red, whereas the reference one is marked in blue.


Figure 2.3D configuration comparison between two variations of the cholesterol oxidase from Chromobacterium sp. The one expressed by the team is left, the reference one is on the right.




 

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