@article {2217,
	title = {Comparison of CryoEM and X-ray structures of dimethylformamidase.},
	journal = {Prog Biophys Mol Biol},
	year = {2020},
	month = {2020 Jul 28},
	abstract = {<p>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\&nbsp;{\textdegree}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.</p>
},
	issn = {1873-1732},
	doi = {10.1016/j.pbiomolbio.2020.06.008},
	author = {Vinothkumar, Kutti R and Arya, Chetan Kumar and Ramanathan, Gurunath and Subramanian, Ramaswamy}
}
