Aconitase is an enzyme participating in the citric acid cycle. It is highly conserved among many species.
It has been shown [1] that it is dually located in mitochondria and the cytosol by means of reverse translocation. To understand the underlying mechanism that enables this phenomena, a structural predicted model has been created using the I-TASSER homology modelling server [2]
Here it is possible to see the bovine aconitase that served as a template for the modeling. It is a large and stable protein with many secondary structures (here the as an example).
Since prior experiments show that the last six residues are crucial for its dual targeting [3], a structural comparison has been performed looking at the .
It was found that an important salt bridge exists in yeast aconitase where a exists instead in bovine aconitase ,in a very conserved area. This difference may be the underlying reason for the difference in the protein's behavior between different species.
