NDLI: Crystallization and preliminary X-ray diffraction analysis of the hyperthermophilic Sulfolobus islandicus lactonase.

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Crystallization and preliminary X-ray diffraction analysis of the hyperthermophilic Sulfolobus islandicus lactonase.

Content Provider	Europe PMC
Author	Gotthard, Guillaume Hiblot, Julien Elias, Mikael Chabrière, Eric
Copyright Year	2011
Description	Phosphotriesterase-like lactonases (PLLs) constitute an interesting family of enzymes that are of paramount interest in biotechnology with respect to their catalytic functions. As natural lactonases, they may act against pathogens such as Pseudomonas aeruginosa by shutting down their quorum-sensing system (quorum quenching) and thus decreasing pathogen virulence. Owing to their promiscuous phosphotriesterase activity, which can inactivate toxic organophosphorus compounds such as pesticides and nerve agents, they are equally appealing as potent bioscavengers. A new representative of the PLL family has been identified (SisPox) and its gene was cloned from the hyperthermophilic archeon Sulfolobus islandicus. Owing to its hyperthermostable architecture, SisPox appears to be a good candidate for engineering studies. Here, production, purification, crystallization conditions and data collection to 2.34 Å resolution are reported for this lactonase from the hyperthermophilic S. islandicus. A lactonase from the hyperthermophilic archaeon S. islandicus has been crystallized. In combination with biochemical and bioengineering studies, it is expected that the structure of this protein will provide insight into the natural function of the phosphotriesterase-like lactonase family.
Related Links	https://europepmc.org/backend/ptpmcrender.fcgi?accid=PMC3053162&blobtype=pdf
Volume Number	67
PubMed Central reference number	PMC3053162
Issue Number	Pt 3
Issue Number	pt 3
PubMed reference number	21393842
Journal	Acta Crystallographica Section F: Structural Biology and Crystallization Communications [Acta Crystallogr Sect F Struct Biol Cryst Commun]
e-ISSN	17443091
DOI	10.1107/s1744309110053819
Language	English
Publisher	International Union of Crystallography
Publisher Date	2011-02-25
Access Restriction	Open
Rights License	© International Union of Crystallography 2011
Subject Keyword	lactonases phosphotriesterases phosphotriesterase-like lactonases quorum sensing quorum quenching bioscavengers hyperthermophiles
Content Type	Text
Resource Type	Article
Subject	Biochemistry Condensed Matter Physics Genetics Biophysics Structural Biology

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