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

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 May 1;61(Pt 5):479-81. doi: 10.1107/S174430910501016X. Epub 2005 Apr 9.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / metabolism
  • Biodegradation, Environmental
  • Biopolymers / chemistry
  • Carboxylic Ester Hydrolases / chemistry*
  • Carboxylic Ester Hydrolases / metabolism
  • Crystallization
  • Crystallography, X-Ray
  • Gram-Negative Bacteria / enzymology*
  • Gram-Negative Bacteria / metabolism
  • Temperature

Substances

  • Bacterial Proteins
  • Biopolymers
  • Carboxylic Ester Hydrolases
  • PHAZ7 protein, Paucimonas lemoignei