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 aminoacids. The predicted secondary structure is the following.

A BLAST was performed for this secuence 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 aminoacids and a very similar structure, which can be observed in the figure below.

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