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Understanding the features of super uranyl binding protein

A paper recently published in the Journal of the American Chemical Society and selected for its JACS Spotlights reports the results of the computational study on the capture of uranyl, UO22+ by the super uranyl binding protein (SUP). This study was performed by Post-doctoral Associate Samuel Odoh, Ph.D., and Graduate Student Gary Bondarevsky in Professor Laura Gagliardi’s lab.

This study shows how UO22+ capture is governed by the nature of the amino acid residues 
in the binding site, the integrity and strength of the second-sphere hydrogen bond 
network, and the number of water molecules in the first coordination sphere. Alteration of
 any of these three factors through mutations generally results in a reduction of the binding 
free energy of UO22+ to the aqueous protein as well as of the difference between the 
binding free energies of UO22+ and other ions such as Ca2+, Cu2+, Mg2+, and Zn2+. As part of this, study a mutant of SUP was computationally discovered, specifically the GLU64ASP mutant, that not only binds UO22+ more strongly than SUP, but that is also more selective for UO22+ over other ions.

The predictions from the computations of the Gagliardi’s group were confirmed by experiments performed in the group of Professor Chuan He 
at the University of Chicago. JACS Spotlights seeks to make published research more accessible to the broader community.