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Title: Crystallization and preliminary X-ray diffraction analysis of the hyperthermophilic Sulfolobus solfataricus phosphotriesterase

Abstract

A phosphotriesterase (PTE) from the hyperthermophilic archaeon S. solfataricus has been crystallized. Combined with biochemical and bioengineering studies, it is expected that the structure of this protein will provide insight into the natural function of the PTE family and provide important data for achieving an efficient organophosphate biodecontaminant. Organophosphates constitute the largest class of insecticides used worldwide and some of them are potent nerve agents. Consequently, organophosphate-degrading enzymes are of paramount interest as they could be used as bioscavengers and biodecontaminants. Phosphotriesterases (PTEs) are capable of hydrolyzing these toxic compounds with high efficiency. A distant and hyperthermophilic representative of the PTE family was cloned from the archeon Sulfolobus solfataricus MT4, overexpressed in Escherichia coli and crystallized; the crystals diffracted to 2.54 Å resolution. Owing to its exceptional thermostability, this PTE may be an excellent candidate for obtaining an efficient organophosphate biodecontaminant. Here, the crystallization conditions and data collection for the hyperthermophilic S. solfataricus PTE are reported.

Authors:
 [1];  [2];  [3];  [1];  [3];  [4];  [3];  [1]
  1. Laboratoire de Cristallographie et Modélisation des Matériaux Minéraux et Biologiques, CNRS-Université Henri Poincaré, 54506 Vandoeuvre-lès-Nancy (France)
  2. Laboratoire de Cristallogenèse et Cristallographie des Protéines, Institut de Biologie Structurale J.-P. Ebel, 38027 Grenoble (France)
  3. Istituto di Biochimica delle Proteine, Consiglio Nazionale delle Ricerche, Via P. Castellino 111, 80131 Napoli (Italy)
  4. Unité d’Enzymologie, Département de Toxicologie, Centre de Recherches du Service de Santé des Armées, 38702 La Tronche (France)
Publication Date:
OSTI Identifier:
22360372
Resource Type:
Journal Article
Journal Name:
Acta Crystallographica. Section F
Additional Journal Information:
Journal Volume: 63; Journal Issue: Pt 7; Other Information: PMCID: PMC2335143; PMID: 17620708; PUBLISHER-ID: ll5109; OAI: oai:pubmedcentral.nih.gov:2335143; Copyright (c) International Union of Crystallography 2007; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 1744-3091
Country of Publication:
United Kingdom
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; CRYSTALLIZATION; CRYSTALS; EFFICIENCY; ESCHERICHIA COLI; RESOLUTION; X-RAY DIFFRACTION

Citation Formats

Elias, Mikael, Dupuy, Jérôme, Merone, Luigia, Lecomte, Claude, Rossi, Mosè, Masson, Patrick, Manco, Giuseppe, Chabriere, Eric, and Unité d’Enzymologie, Département de Toxicologie, Centre de Recherches du Service de Santé des Armées, 38702 La Tronche. Crystallization and preliminary X-ray diffraction analysis of the hyperthermophilic Sulfolobus solfataricus phosphotriesterase. United Kingdom: N. p., 2007. Web. doi:10.1107/S1744309107023512.
Elias, Mikael, Dupuy, Jérôme, Merone, Luigia, Lecomte, Claude, Rossi, Mosè, Masson, Patrick, Manco, Giuseppe, Chabriere, Eric, & Unité d’Enzymologie, Département de Toxicologie, Centre de Recherches du Service de Santé des Armées, 38702 La Tronche. Crystallization and preliminary X-ray diffraction analysis of the hyperthermophilic Sulfolobus solfataricus phosphotriesterase. United Kingdom. https://doi.org/10.1107/S1744309107023512
Elias, Mikael, Dupuy, Jérôme, Merone, Luigia, Lecomte, Claude, Rossi, Mosè, Masson, Patrick, Manco, Giuseppe, Chabriere, Eric, and Unité d’Enzymologie, Département de Toxicologie, Centre de Recherches du Service de Santé des Armées, 38702 La Tronche. 2007. "Crystallization and preliminary X-ray diffraction analysis of the hyperthermophilic Sulfolobus solfataricus phosphotriesterase". United Kingdom. https://doi.org/10.1107/S1744309107023512.
@article{osti_22360372,
title = {Crystallization and preliminary X-ray diffraction analysis of the hyperthermophilic Sulfolobus solfataricus phosphotriesterase},
author = {Elias, Mikael and Dupuy, Jérôme and Merone, Luigia and Lecomte, Claude and Rossi, Mosè and Masson, Patrick and Manco, Giuseppe and Chabriere, Eric and Unité d’Enzymologie, Département de Toxicologie, Centre de Recherches du Service de Santé des Armées, 38702 La Tronche},
abstractNote = {A phosphotriesterase (PTE) from the hyperthermophilic archaeon S. solfataricus has been crystallized. Combined with biochemical and bioengineering studies, it is expected that the structure of this protein will provide insight into the natural function of the PTE family and provide important data for achieving an efficient organophosphate biodecontaminant. Organophosphates constitute the largest class of insecticides used worldwide and some of them are potent nerve agents. Consequently, organophosphate-degrading enzymes are of paramount interest as they could be used as bioscavengers and biodecontaminants. Phosphotriesterases (PTEs) are capable of hydrolyzing these toxic compounds with high efficiency. A distant and hyperthermophilic representative of the PTE family was cloned from the archeon Sulfolobus solfataricus MT4, overexpressed in Escherichia coli and crystallized; the crystals diffracted to 2.54 Å resolution. Owing to its exceptional thermostability, this PTE may be an excellent candidate for obtaining an efficient organophosphate biodecontaminant. Here, the crystallization conditions and data collection for the hyperthermophilic S. solfataricus PTE are reported.},
doi = {10.1107/S1744309107023512},
url = {https://www.osti.gov/biblio/22360372}, journal = {Acta Crystallographica. Section F},
issn = {1744-3091},
number = Pt 7,
volume = 63,
place = {United Kingdom},
year = {Sun Jul 01 00:00:00 EDT 2007},
month = {Sun Jul 01 00:00:00 EDT 2007}
}