1EZ2
THREE-DIMENSIONAL STRUCTURE OF THE ZINC-CONTAINING PHOSPHOTRIESTERASE WITH BOUND SUBSTRATE ANALOG DIISOPROPYLMETHYL PHOSPHONATE.
Summary for 1EZ2
| Entry DOI | 10.2210/pdb1ez2/pdb |
| Related | 1EYW |
| Descriptor | PHOSPHOTRIESTERASE, ZINC ION, METHYLPHOSPHONIC ACID DIISOPROPYL ESTER, ... (4 entities in total) |
| Functional Keywords | hydrolase zinc organophosphate, hydrolase |
| Biological source | Brevundimonas diminuta |
| Cellular location | Cell membrane; Peripheral membrane protein: P0A434 |
| Total number of polymer chains | 2 |
| Total formula weight | 72541.92 |
| Authors | Holden, H.M.,Benning, M.M.,Raushel, F.M.,Hong, S.-B. (deposition date: 2000-05-09, release date: 2000-12-20, Last modification date: 2025-03-26) |
| Primary citation | Benning, M.M.,Hong, S.B.,Raushel, F.M.,Holden, H.M. The binding of substrate analogs to phosphotriesterase. J.Biol.Chem., 275:30556-30560, 2000 Cited by PubMed Abstract: Phosphotriesterase (PTE) from Pseudomonas diminuta catalyzes the detoxification of organophosphates such as the widely utilized insecticide paraoxon and the chemical warfare agent sarin. The three-dimensional structure of the enzyme is known from high resolution x-ray crystallographic analyses. Each subunit of the homodimer folds into a so-called TIM barrel, with eight strands of parallel beta-sheet. The two zinc ions required for activity are positioned at the C-terminal portion of the beta-barrel. Here, we describe the three-dimensional structure of PTE complexed with the inhibitor diisopropyl methyl phosphonate, which serves as a mimic for sarin. Additionally, the structure of the enzyme complexed with triethyl phosphate is also presented. In the case of the PTE-diisopropyl methyl phosphonate complex, the phosphoryl oxygen of the inhibitor coordinates to the more solvent-exposed zinc ion (2.5 A), thereby lending support to the presumed catalytic mechanism involving metal coordination of the substrate. In the PTE-triethyl phosphate complex, the phosphoryl oxygen of the inhibitor is positioned at 3.4 A from the more solvent-exposed zinc ion. The two structures described in this report provide additional molecular understanding for the ability of this remarkable enzyme to hydrolyze such a wide range of organophosphorus substrates. PubMed: 10871616DOI: 10.1074/jbc.M003852200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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