2VC7
Structural basis for natural lactonase and promiscuous phosphotriesterase activities
Summary for 2VC7
| Entry DOI | 10.2210/pdb2vc7/pdb |
| Related | 2VC5 |
| Descriptor | ARYLDIALKYLPHOSPHATASE, FE (II) ION, COBALT (II) ION, ... (7 entities in total) |
| Functional Keywords | phosphotriesterase, promiscuous activities, enzyme evolution, hyperthermophilic, lactonase, hydrolase, biotechnology, quorum sensing |
| Biological source | SULFOLOBUS SOLFATARICUS |
| Total number of polymer chains | 4 |
| Total formula weight | 148306.74 |
| Authors | Elias, M.,Dupuy, J.,Merone, L.,Mandrich, L.,Moniot, S.,Rochu, D.,Lecomte, C.,Rossi, M.,Masson, P.,Manco, G.,Chabriere, E. (deposition date: 2007-09-19, release date: 2008-04-15, Last modification date: 2023-12-13) |
| Primary citation | Elias, M.,Dupuy, J.,Merone, L.,Mandrich, L.,Porzio, E.,Moniot, S.,Rochu, D.,Lecomte, C.,Rossi, M.,Masson, P.,Manco, G.,Chabriere, E. Structural Basis for Natural Lactonase and Promiscuous Phosphotriesterase Activities. J.Mol.Biol., 379:1017-, 2008 Cited by PubMed Abstract: Organophosphates are the largest class of known insecticides, several of which are potent nerve agents. Consequently, organophosphate-degrading enzymes are of great scientific interest as bioscavengers and biodecontaminants. Recently, a hyperthermophilic phosphotriesterase (known as SsoPox), from the Archaeon Sulfolobus solfataricus, has been isolated and found to possess a very high lactonase activity. Here, we report the three-dimensional structures of SsoPox in the apo form (2.6 A resolution) and in complex with a quorum-sensing lactone mimic at 2.0 A resolution. The structure also reveals an unexpected active site topology, and a unique hydrophobic channel that perfectly accommodates the lactone substrate. Structural and mutagenesis evidence allows us to propose a mechanism for lactone hydrolysis and to refine the catalytic mechanism established for phosphotriesterases. In addition, SsoPox structures permit the correlation of experimental lactonase and phosphotriesterase activities and this strongly suggests lactonase activity as the cognate function of SsoPox. This example demonstrates that promiscuous activities probably constitute a large and efficient reservoir for the creation of novel catalytic activities. PubMed: 18486146DOI: 10.1016/J.JMB.2008.04.022 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.05 Å) |
Structure validation
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