Crystallization and preliminary X-ray analysis of alginate lyase, a member of family PL-7, from Pseudomonas aeruginosa

Acta Crystallogr D Biol Crystallogr. 2003 Aug;59(Pt 8):1499-501. doi: 10.1107/s0907444903012836. Epub 2003 Jul 23.

Abstract

Alginate lyase depolymerizes alginate, a heteropolysaccharide consisting of alpha-L-guluronate and beta-D-mannuronate, through a beta-elimination reaction. A protein PA1167 with a molecular mass of 25 kDa produced by Pseudomonas aeruginosa is an alginate lyase classified into polysaccharide lyase family PL-7. The enzyme was crystallized at 293 K in a drop solution comprising 1.4 M sodium chloride, 0.1 M potassium sodium phosphate and 0.1 M 2-morpholinoethanesulfonate-sodium hydroxide pH 6.5 by means of the vapor-diffusion method. The crystals were monoclinic and belonged to space group P2(1), with unit-cell parameters a = 43.4, b = 70.3, c = 67.4 A, beta = 94.5 degrees. Diffraction data were collected to 2.0 A from a single crystal.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Carbohydrate Sequence
  • Crystallization
  • Crystallography, X-Ray
  • Escherichia coli / metabolism
  • Models, Chemical
  • Molecular Sequence Data
  • Phosphates / chemistry
  • Polysaccharide-Lyases / chemistry*
  • Potassium / chemistry
  • Pseudomonas aeruginosa / enzymology*
  • Sodium Chloride / chemistry
  • Sodium Hydroxide / chemistry
  • Temperature
  • X-Rays

Substances

  • Phosphates
  • Sodium Chloride
  • Sodium Hydroxide
  • Polysaccharide-Lyases
  • poly(beta-D-mannuronate) lyase
  • Potassium
  • sodium phosphate