5G4H
Target information
- RCSB PDB
- 5G4H
- Title
- 1.50 A resolution catechol (1,2-dihydroxybenzene) inhibited Sporosarcina pasteurii urease
- Method
- X-RAY DIFFRACTION
- Resolution
- 1.5
- Classification
- HYDROLASE
- Organism
- Sporosarcina pasteurii
- Protein
- Urease subunit gamma (P41022)
- Year
- 2016
- Publication Title
- Inactivation of Urease by Catechol: Kinetics and Structure.
- Abstract
-
Urease is a Ni(II)-containing enzyme that catalyzes the hydrolysis of urea to yield ammonia and carbamate at a rate 10 15 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 1.50? resolution, reveals the structural details of the enzyme inhibition.
- External Link
- RCSB PDB
Ligand information
- HET
- CAQ
- Chain ID
- C
- HET Number
- 1571
- Molecular Formula
- C6H6O2
- Structure
-
- IUPAC Name
- benzene-1,2-diol
- InChI
- InChI=1S/C6H6O2/c7-5-3-1-2-4-6(5)8/h1-4,7-8H
- InChI Key
- YCIMNLLNPGFGHC-UHFFFAOYSA-N
- Canonical SMILES
- Oc1ccccc1O
- Bioactivity data
- CI005252
Covalent Binding
- Warhead
- Catechol
- Reaction Mechanism
- Nucleophilic Substitution
- Residue
- CYS : 322
- Residue Chain
- C
- Interactions