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

被引:17
作者
Elias, Mikael
Dupuy, Jerome
Merone, Luigia
Lecomte, Claude
Rossi, Mose
Masson, Patrick
Manco, Giuseppe
Chabriere, Eric [1 ]
机构
[1] Univ Henri Poincare, CNRS, Lab Cristallograph & Modelisat Mat Mineraux & Bio, F-54506 Vandoeuvre Les Nancy, France
[2] Inst Biol Struct JP Ebel, Lab Crystallogenese & Crystallograph Protein, F-38027 Grenoble, France
[3] CNR, Ist Biochim Protein, I-80131 Naples, Italy
[4] Ctr Rech Serv St Armees, Dept Toxicol, Unit Enzymol, La Tronche, France
来源
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2007年 / 63卷
关键词
D O I
10.1107/S1744309107023512
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
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 angstrom 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.
引用
收藏
页码:553 / 555
页数:3
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