Structural insights into how GTP-dependent conformational changes in a metallochaperone UreG facilitate urease maturation [Biochemistry]

The ability of metallochaperones to allosterically regulate the binding/release of metal ions and to switch protein-binding partners along the metal delivery pathway is essential to the metallation of the metalloenzymes. Urease, catalyzing the hydrolysis of urea into ammonia and carbon dioxide, contains two nickel ions bound by a carbamylated lysine...

http://ift.tt/2yZ50dz