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.

http://pubs.acs.org/doi/abs/10.1021/ja5087563 JACS Spotlights seeks to make published research more accessible to the broader community.