Title : Crystallization and preliminary X-ray analysis of a novel thermoalkalophilic poly(3-hydroxybutyrate) depolymerase (PhaZ7) from Paucimonas lemoignei - Kapetaniou_2005_Acta.Crystallogr.Sect.F.Struct.Biol.Cryst.Commun_61_479 |
Author(s) : Kapetaniou EG , Braaz R , Jendrossek D , Papageorgiou AC |
Ref : Acta Crystallographica Sect F Struct Biol Cryst Commun , 61 :479 , 2005 |
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. |
PubMedSearch : Kapetaniou_2005_Acta.Crystallogr.Sect.F.Struct.Biol.Cryst.Commun_61_479 |
PubMedID: 16511073 |
Gene_locus related to this paper: psele-PHAZ7 |
Substrate | P(3HO) |
Gene_locus | psele-PHAZ7 |
Family | PHAZ7_phb_depolymerase |
Structure | 2VTV |
Kapetaniou EG, Braaz R, Jendrossek D, Papageorgiou AC (2005)
Crystallization and preliminary X-ray analysis of a novel thermoalkalophilic poly(3-hydroxybutyrate) depolymerase (PhaZ7) from Paucimonas lemoignei
Acta Crystallographica Sect F Struct Biol Cryst Commun
61 :479
Kapetaniou EG, Braaz R, Jendrossek D, Papageorgiou AC (2005)
Acta Crystallographica Sect F Struct Biol Cryst Commun
61 :479