5G4H
1.50 A resolution catechol (1,2-dihydroxybenzene) inhibited Sporosarcina pasteurii urease
Summary for 5G4H
| Entry DOI | 10.2210/pdb5g4h/pdb |
| Descriptor | UREASE SUBUNIT GAMMA, UREASE SUBUNIT BETA, UREASE SUBUNIT ALPHA, ... (9 entities in total) |
| Functional Keywords | hydrolase |
| Biological source | SPOROSARCINA PASTEURII More |
| Cellular location | Cytoplasm : A0A0H3YGY5 A0A0H3YLV6 A0A0H3YL32 |
| Total number of polymer chains | 3 |
| Total formula weight | 88437.98 |
| Authors | Mazzei, L.,Cianci, M.,Musiani, F.,Ciurli, S. (deposition date: 2016-05-13, release date: 2016-12-07, Last modification date: 2024-01-10) |
| Primary citation | Mazzei, L.,Cianci, M.,Musiani, F.,Lente, G.,Palombo, M.,Ciurli, S. Inactivation of Urease by Catechol: Kinetics and Structure. J.Inorg.Biochem., 166:182-, 2016 Cited by PubMed Abstract: Urease is a Ni(II)-containing enzyme that catalyzes the hydrolysis of urea to yield ammonia and carbamate at a rate 10 times higher than the uncatalyzed reaction. Urease is a virulence factor of several human pathogens, in addition to decreasing the efficiency of soil organic nitrogen fertilization. Therefore, efficient urease inhibitors are actively sought. In this study, we describe a molecular characterization of the interaction between urease from Sporosarcina pasteurii (SPU) and Canavalia ensiformis (jack bean, JBU) with catechol, a model polyphenol. In particular, catechol irreversibly inactivates both SPU and JBU with a complex radical-based autocatalytic multistep mechanism. The crystal structure of the SPU-catechol complex, determined at 1.50Å resolution, reveals the structural details of the enzyme inhibition. PubMed: 27888701DOI: 10.1016/J.JINORGBIO.2016.11.016 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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