Crystallization and preliminary X-ray analysis of a novel thermoalkalophilic poly(3-hydroxybutyrate) depolymerase (PhaZ7) from Paucimonas lemoignei

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
Evangelia G KapetaniouAnastassios C Papageorgiou

Abstract

Polyhydroxyalkanoates (PHA) are biodegradable polyesters that have attracted commercial and academic interest as environmentally friendly materials. A number of enzymes are able to degrade polyhydroxyalkanoates to water-soluble products. PhaZ7 poly(3-hydroxybutyrate) (PHB) depolymerase (EC 3.1.1.75), a 342-amino-acid hydrolase from the PHA-degrading bacterium Paucimonas lemoignei, has been found to possess substrate specificity for amorphous PHA. PhaZ7 was crystallized by the microdialysis method. Thin rod-like crystals were grown in low ionic strength solution and found to belong to the monoclinic space group C2, with unit-cell parameters a = 225.8, b = 46.5, c = 171.3, beta = 128.9 degrees. A complete data set was collected to 2.75 A resolution at 100 K using synchrotron radiation.

References

Apr 28, 1968·Journal of Molecular Biology·B W Matthews
Sep 6, 2002·Annual Review of Microbiology·Dieter Jendrossek, Rene Handrick

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Citations

Jun 3, 2010·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Sachin WakadkarAnastassios C Papageorgiou
Aug 19, 2008·Journal of Molecular Biology·Anastassios C PapageorgiouDieter Jendrossek
Jun 19, 2007·Applied and Environmental Microbiology·Alberto QuesadaRafael Blasco

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