Comparison of CryoEM and X-ray structures of dimethylformamidase.
|Title||Comparison of CryoEM and X-ray structures of dimethylformamidase.|
|Publication Type||Journal Article|
|Year of Publication||2020|
|Authors||Vinothkumar KR, Arya CKumar, Ramanathan G, Subramanian R|
|Journal||Prog Biophys Mol Biol|
|Date Published||2020 Jul 28|
Dimethylformamidase (DMFase) catalyzes the hydrolysis of dimethylformamide, an industrial solvent, introduced into the environment by humans. Recently, we determined the structures of dimethylformamidase by electron cryo microscopy and X-ray crystallography revealing a tetrameric enzyme with a mononuclear iron at the active site. DMFase from Paracoccus sp. isolated from a waste water treatment plant around the city of Kanpur in India shows maximal activity at 54 °C and is halotolerant. The structures determined by both techniques are mostly identical and the largest difference is in a loop near the active site. This loop could play a role in co-operativity between the monomers. A number of non-protein densities are observed in the EM map, which are modelled as water molecules. Comparison of the structures determined by the two methods reveals conserved water molecules that could play a structural role. The higher stability, unusual active site and negligible activity at low temperature makes this a very good model to study enzyme mechanism by cryoEM.
|Alternate Journal||Prog Biophys Mol Biol|