Team:ITESM-CEM/Cholesterol

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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;">Cholesterol Oxidase</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/Oxoacyl" style="color: #FFF;">Oxoacyl Reductase</a></sub>  
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      <sub><a href="https://2014.igem.org/Team:ITESM-CEM/CholesterolOxidase">Cholesterol Oxidase</a></sub>
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       <sub><a href="https://2014.igem.org/Team:ITESM-CEM/Oxoacyl">Oxoacyl Reductase</a></sub>  
       <sub><a href="https://2014.igem.org/Team:ITESM-CEM/Cholesterol" style="color: #FFF;">7-Dehydratase</a></sub>
       <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/EnzymaticKinectics">Enzymatic Kinetics</a></sub>
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<!--INICIO CONTENIDO-->
<!--INICIO CONTENIDO-->
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<h2>Subtítulo 1</h2>
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<h2>7-Dehydratase</h2>
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       <p>If you choose to create a model during your project, please write about it here. Modeling is not an essential part of iGEM, but we encourage any and all teams to model some aspect of their project. See previous "Best Model" awards for more information.</p>
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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 -0.03 C-score which makes it, out of the 4 predicted models, the more plausible to be the actual three dimensional conformation of the protein.</p>
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      <h2>Subtítulo 2</h2>
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      <p>Nulla porttitor aliquet elit, vel mollis sem malesuada sit amet. Cum sociis natoque penatibus et magnis dis parturient montes, nascetur ridiculus mus. Morbi vitae fermentum turpis. Suspendisse laoreet, elit quis pretium pharetra, est quam viverra ipsum, ac laoreet erat urna a odio. Quisque condimentum nibh erat, sed vulputate eros dictum vel. Cum sociis natoque penatibus et magnis dis parturient montes, nascetur ridiculus mus. Suspendisse viverra mauris sed adipiscing adipiscing. Proin egestas placerat sem, varius pretium est aliquam et. Etiam mattis mattis dolor, suscipit gravida lectus blandit a. Donec felis dui, venenatis lobortis ullamcorper at, consectetur et massa.
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<p class="centeredImage"><img src="https://static.igem.org/mediawiki/2014/2/2c/Imagenes_enzimas_modelado-7.jpg" height="304" width="321" hspace="10" BORDER=10></p><br>
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<br><br><br><br>
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</p>
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<p style="text-align: justify; text-justify: inter-word;">The theoretical dehydratase has 179 amino acids. The predicted secondary structure is the following.</p><br>
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<p class="centeredImage"><img src="https://static.igem.org/mediawiki/2014/5/55/Imagenes_enzimas_modelado-1.jpg" height="200" width="650" hspace="10" BORDER=10></p><br>
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<p style="text-align: justify; text-justify: inter-word;">A BLAST was performed for this sequence to find molecules with similar structures and functions. However, most of the secuences found were uncharacterized molecules. The closest characterized molecule found was the Bile acid 7-alpha dehydratase form Clostridium hiranonis. It has a 51% identity which is not ideal, but all together it has 129 similar amino acids and a very similar structure, which can be observed in the figure below. </p><br>
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<p class="centeredImage"><img src="https://static.igem.org/mediawiki/2014/a/a4/Imagenes_enzimas_modelado-13.jpg" width="390" height="203" hspace="10" BORDER=10></p><br>
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<p><pie><b>Figure 1.</b>3D configuration comparison between the theoretical dehydrogenase from Rhodococcus jostii (right) and the Bile acid 7-alpha dehydratase form Clostridium hiranonis (left). </pie></p>
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<p style="text-align: justify; text-justify: inter-word;">The information found in RCSB (http://www.rcsb.org/pdb/explore/explore.do?structureId=4N3V) revealed that this protein works in homo 3-mers. Eventhough it has a very similar structure, it must be noted that the fucntions of these two enzymes are different and therefor it cannot be assumed safely that the dehydrogenase from Rhodococcus jostii will also work in homo 3-mers.</p>
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      <h2>Physicochemical Characteristics</h2>
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<p><pie><b>Table 1.</b> Theoretical dehydrogenase physicochemical characteristics obtained from XTalPred-RF. </pie></p>
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<p class="centeredImage"><img src="https://static.igem.org/mediawiki/2014/b/b9/Tabla3.JPG" hspace="10" BORDER=10></p><br>
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<!--FIN CONTENIDO-->
<!--FIN CONTENIDO-->

Latest revision as of 16:12, 14 October 2014

TEC-CEM | Modeling

ITESM-CEM | Enzy7-K me

Modeling 3325

 

7-Dehydratase

This tridimensional model was obtained with the I-TASSER software. It has a -0.03 C-score which makes it, out of the 4 predicted models, the more plausible to be the actual three dimensional conformation of the protein.


The theoretical dehydratase has 179 amino acids. The predicted secondary structure is the following.



A BLAST was performed for this sequence to find molecules with similar structures and functions. However, most of the secuences found were uncharacterized molecules. The closest characterized molecule found was the Bile acid 7-alpha dehydratase form Clostridium hiranonis. It has a 51% identity which is not ideal, but all together it has 129 similar amino acids and a very similar structure, which can be observed in the figure below.



Figure 1.3D configuration comparison between the theoretical dehydrogenase from Rhodococcus jostii (right) and the Bile acid 7-alpha dehydratase form Clostridium hiranonis (left).

The information found in RCSB (http://www.rcsb.org/pdb/explore/explore.do?structureId=4N3V) revealed that this protein works in homo 3-mers. Eventhough it has a very similar structure, it must be noted that the fucntions of these two enzymes are different and therefor it cannot be assumed safely that the dehydrogenase from Rhodococcus jostii will also work in homo 3-mers.

Physicochemical Characteristics

Table 1. Theoretical dehydrogenase physicochemical characteristics obtained from XTalPred-RF.