2KAU

THE CRYSTAL STRUCTURE OF UREASE FROM KLEBSIELLA AEROGENES AT 2.2 ANGSTROMS RESOLUTION

Summary for 2KAU

• Entry DOI: 10.2210/pdb2kau/pdb
• Descriptor: UREASE (GAMMA CHAIN), UREASE (BETA CHAIN), UREASE (ALPHA CHAIN), ... (5 entities in total)
• Functional Keywords: nickel metalloenzyme, hydrolase (urea amido), hydrolase
• Biological source: Klebsiella aerogenes; More
• Cellular location: Cytoplasm (By similarity): P18316 P18315 P18314
• Total number of polymer chains: 3
• Total formula weight: 83339.90

Authors

Jabri, E.,Carr, M.B.,Hausinger, R.P.,Karplus, P.A. (deposition date: 1995-02-16, release date: 1995-07-10, Last modification date: 2024-06-05)

Primary citation

Jabri, E.,Carr, M.B.,Hausinger, R.P.,Karplus, P.A.
The crystal structure of urease from Klebsiella aerogenes.
Science, 268:998-1004, 1995

PubMed 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.

PubMed: 7754395

Experimental method

X-RAY DIFFRACTION (2 Å)