Nickel management by the accessory protein UreG during urease activation

Le résumé fourni par la source

Computational study of the intrinsically disordered GTPase UreG from Klebsiella pneumoniae, a key factor in urease maturation and Ni(II) trafficking. All-atom molecular dynamics simulations in explicit solvent were performed to investigate the effect of GTP hydrolysis on nickel binding and protein structural dynamics. In total, three 10 µs replicas were carried out for both the GTP-bound and GDP-bound states. Additionally, the final frame of the second GDP-bound replica was used as the starting point for three further 10 µs simulations, to specifically assess the impact of the destabilization of the hydrogen-bond network, characteristic of the GDP-bound statw, linking the nucleotide-binding site to the Cys-Pro-His (CPH) motif.

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