ArticleExtremophiles : life under extreme conditions2009
Structural determinants of the high thermal stability of SsoPox from the hyperthermophilic archaeon Sulfolobus solfataricus.
Article in Extremophiles : life under extreme conditions, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 64 citations in OpenAlex.
- Role of Php domain and related enzymes in the enzymatic degradation of G-series nerve agents.Molecular genetics and genomics : MGG · 2025Review
- Changes in Active Site Loop Conformation Relate to the Transition toward a Novel Enzymatic Activity.JACS Au · 2024Article
- Lactonase-mediated inhibition of quorum sensing largely alters phenotypes, proteome, and antimicrobial activities inFrontiers in cellular and infection microbiology · 2023Article
- Unveiling the Impact of Antibiotics and Alternative Methods for Animal Husbandry: A Review.Antibiotics (Basel, Switzerland) · 2021Review
- Enzymes, Reacting with Organophosphorus Compounds as Detoxifiers: Diversity and Functions.International journal of molecular sciences · 2021Review
- Structural and Functional Characterization of New SsoPox Variant Points to the Dimer Interface as a Driver for the Increase in Promiscuous Paraoxonase Activity.International journal of molecular sciences · 2020Article
- Signal Disruption Leads to Changes in Bacterial Community Population.Frontiers in microbiology · 2019Article
- Stabilizing HIV-1 envelope glycoprotein trimers to induce neutralizing antibodies.Retrovirology · 2018Review
- Modification and Assembly of a Versatile Lactonase for Bacterial Quorum Quenching.Molecules (Basel, Switzerland) · 2018Article
- Rational engineering of a native hyperthermostable lactonase into a broad spectrum phosphotriesterase.Scientific reports · 2017Article
- The quorum-quenching lactonase from Alicyclobacter acidoterrestris: purification, kinetic characterization, crystallization and crystallographic analysis.Acta crystallographica. Section F, Structural biology communications · 2017Article
- Multifactorial level of extremostability of proteins: can they be exploited for protein engineering?Extremophiles : life under extreme conditions · 2017Review
- Engineering of a thermostable esterase Est816 to improve its quorum-quenching activity and the underlying structural basis.Scientific reports · 2016Article
- Organophosphate-Hydrolyzing Enzymes as First-Line of Defence Against Nerve Agent-Poisoning: Perspectives and the Road Ahead.The protein journal · 2016Review
- Harnessing hyperthermostable lactonase from Sulfolobus solfataricus for biotechnological applications.Scientific reports · 2016Article
- The quorum-quenching lactonase from Geobacillus caldoxylosilyticus: purification, characterization, crystallization and crystallographic analysis.Acta crystallographica. Section F, Structural biology communications · 2016Article
- Current and emerging strategies for organophosphate decontamination: special focus on hyperstable enzymes.Environmental science and pollution research international · 2016Review
- Crystal structure of VmoLac, a tentative quorum quenching lactonase from the extremophilic crenarchaeon Vulcanisaeta moutnovskia.Scientific reports · 2015Article
- SacPox from the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius is a proficient lactonase.BMC research notes · 2014Article
- Crystallization and preliminary X-ray diffraction analysis of the lactonase VmoLac from Vulcanisaeta moutnovskia.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013Article
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Authors and funding
13 authors at 8 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Organophosphates (OPs) constitute the largest class of insecticides used worldwide and certain of them are potent nerve agents. Consequently, enzymes degrading OPs are of paramount interest, as they could be used as bioscavengers and biodecontaminants. Looking for a stable OPs catalyst, able to support industrial process constraints, a hyperthermophilic phosphotriesterase (PTE) (SsoPox) was isolated from the archaeon Sulfolobus solfataricus and was found to be highly thermostable. The solved 3D structure revealed that SsoPox is a noncovalent dimer, with lactonase activity against "quorum sensing signals", and therefore could represent also a potential weapon against certain pathogens. The structural basis of the high thermostability of SsoPox has been investigated by performing a careful comparison between its structure and that of two mesophilic PTEs from Pseudomonas diminuta and Agrobacterium radiobacter. In addition, the conformational stability of SsoPox against the denaturing action of temperature and GuHCl has been determined by means of circular dichroism and fluorescence measurements. The data suggest that the two fundamental differences between SsoPox and the mesophilic counterparts are: (a) a larger number of surface salt bridges, also involved in complex networks; (b) a tighter quaternary structure due to an optimization of the interactions at the interface between the two monomers.
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