1. Comparison of CryoEM and X-ray structures of dimethylformamidase.
- Author
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Vinothkumar, Kutti R., Arya, Chetan Kumar, Ramanathan, Gurunath, and Subramanian, Ramaswamy
- Subjects
- *
SEWAGE disposal plants , *X-ray crystallography , *X-ray microscopy , *X-rays , *ELECTRON microscopy , *HUMAN ecology - Abstract
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. [ABSTRACT FROM AUTHOR]
- Published
- 2021
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