Crystallization and preliminary X-ray analysis of a novel thermoalkalophilic poly(3-hydroxybutyrate) depolymerase (PhaZ7) from Paucimonas lemoignei.
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.
Kapetaniou
Evangelia G
EG
Turku Centre for Biotechnology, University of Turku, Tykistökatu 6, Turku 20521, Finland.
Braaz
Reinhard
R
Jendrossek
Dieter
D
Papageorgiou
Anastassios C
AC
D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D001673:Biodegradation, Environmental; D001704:Biopolymers / Q000737:chemistry; D002265:Carboxylic Ester Hydrolases / Q000737:chemistry* / Q000378:metabolism; D003460:Crystallization; D018360:Crystallography, X-Ray; D006090:Gram-Negative Bacteria / Q000201:enzymology* / Q000378:metabolism; D013696:Temperature
D001426:Bacterial Proteins; D001704:Biopolymers; D002265:Carboxylic Ester Hydrolases; C438011:PHAZ7 protein, Paucimonas lemoignei