The crystal structure of urease from Klebsiella aerogenes.

Abstract

The crystal structure of urease from Klebsiella aerogenes has been determined at 2.2 A resolution and refined to an R factor of 18.2 percent. The enzyme contains four structural domains: three with novel folds playing structural roles, and an (alpha beta)8 barrel domain, which contains the bi-nickel center. The two active site nickels are 3.5 A apart. One nickel ion is coordinated by three ligands (with low occupancy of a fourth ligand) and the second is coordinated by five ligands. A carbamylated lysine provides an oxygen ligand to each nickel, explaining why carbon dioxide is required for the activation of urease apoenzyme. The structure is compatible with a catalytic mechanism whereby urea ligates Ni-1 to complete its tetrahedral coordination and a hydroxide ligand of Ni-2 attacks the carbonyl carbon. A surprisingly high structural similarity between the urease catalytic domain and that of the zinc-dependent adenosine deaminase reveals a remarkable example of active site divergence.

050100'97'99'01'03'05'07'09'11'13'15'17
Citations per Year

782 Citations

Semantic Scholar estimates that this publication has 782 citations based on the available data.

See our FAQ for additional information.

Cite this paper

@article{Jabri1995TheCS, title={The crystal structure of urease from Klebsiella aerogenes.}, author={Evelyn Jabri and Molly B Carr and Robert P. Hausinger and P. Andrew Karplus}, journal={Science}, year={1995}, volume={268 5213}, pages={998-1004} }