5VEJ
High resolution crystal structure of a fluoride-inhibited organo-phosphate-degrading metallohydrolase
Summary for 5VEJ
| Entry DOI | 10.2210/pdb5vej/pdb |
| Descriptor | Phosphotriesterase, ACETATE ION, COBALT (II) ION, ... (5 entities in total) |
| Functional Keywords | metallohydrolase, fluoride, inhibited, organo-phosphate-degrading, hydrolase |
| Biological source | Rhizobium radiobacter (Agrobacterium tumefaciens) |
| Total number of polymer chains | 1 |
| Total formula weight | 35843.48 |
| Authors | Selleck, C. (deposition date: 2017-04-04, release date: 2017-07-19, Last modification date: 2023-11-15) |
| Primary citation | Selleck, C.,Guddat, L.W.,Ollis, D.L.,Schenk, G.,Pedroso, M.M. High resolution crystal structure of a fluoride-inhibited organophosphate-degrading metallohydrolase. J. Inorg. Biochem., 177:287-290, 2017 Cited by PubMed Abstract: Metal ion-dependent, organophosphate-degrading enzymes (OP hydrolases) have received increasing attention due to their ability to degrade and thus detoxify commonly used pesticides and nerve agents such as sarin and VX. These enzymes thus garner strong potential as bioremediators. The OP hydrolase from Agrobacterium radiobacter (OpdA) is one of the most efficient members of this group of enzymes. Previous studies have indicated that the choice of the hydrolysis-initiating nucleophile may depend on the pH of the reaction, with a metal ion-bridging hydroxide being preferred at lower pH (i.e. pH≤8.5), and a terminally coordinated hydroxide at higher pH (i.e. pH>9.0). Furthermore, fluoride was shown to be a potent inhibitor of the reaction, but only at low pH. Here, the crystal structure (1.3Å, pH6) of OpdA in presence of fluoride is described. While the first coordination sphere in the active site displays minimal changes in the presence of fluoride, the hydrogen bonding network that connects the dimetallic metal center to the substrate binding pocket is disrupted. Thus, the structure of fluoride-inhibited OpdA demonstrates the significance of this hydrogen bond network in controlling the mechanism and function of this enzyme. PubMed: 28673485DOI: 10.1016/j.jinorgbio.2017.06.013 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.301 Å) |
Structure validation
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