4AC7
The crystal structure of Sporosarcina pasteurii urease in complex with citrate
Summary for 4AC7
| Entry DOI | 10.2210/pdb4ac7/pdb |
| Related | 1IE7 1S3T 1UBP 2UBP 3UBP 4UBP |
| Descriptor | UREASE SUBUNIT GAMMA, UREASE SUBUNIT BETA, UREASE SUBUNIT ALPHA, ... (9 entities in total) |
| Functional Keywords | hydrolase, bacillus pasteurii |
| Biological source | SPOROSARCINA PASTEURII More |
| Cellular location | Cytoplasm : P41022 P41021 P41020 |
| Total number of polymer chains | 3 |
| Total formula weight | 88155.72 |
| Authors | Benini, S.,Kosikowska, P.,Cianci, M.,Gonzalez Vara, A.,Berlicki, L.,Ciurli, S. (deposition date: 2011-12-14, release date: 2013-01-16, Last modification date: 2023-12-20) |
| Primary citation | Benini, S.,Kosikowska, P.,Cianci, M.,Mazzei, L.,Vara, A.G.,Berlicki, L.,Ciurli, S. The Crystal Structure of Sporosarcina Pasteurii Urease in a Complex with Citrate Provides New Hints for Inhibitor Design. J.Biol.Inorg.Chem., 18:391-, 2013 Cited by PubMed Abstract: Urease, the enzyme that catalyses the hydrolysis of urea, is a virulence factor for a large number of ureolytic bacterial human pathogens. The increasing resistance of these pathogens to common antibiotics as well as the need to control urease activity to improve the yield of soil nitrogen fertilization in agricultural applications has stimulated the development of novel classes of molecules that target urease as enzyme inhibitors. We report on the crystal structure at 1.50-Å resolution of a complex formed between citrate and urease from Sporosarcina pasteurii, a widespread and highly ureolytic soil bacterium. The fit of the ligand to the active site involves stabilizing interactions, such as a carboxylate group that binds the nickel ions at the active site and several hydrogen bonds with the surrounding residues. The citrate ligand has a significantly extended structure compared with previously reported ligands co-crystallized with urease and thus represents a unique and promising scaffold for the design of new, highly active, stable, selective inhibitors. PubMed: 23412551DOI: 10.1007/S00775-013-0983-7 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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