Purification, co-crystallization and preliminary X--ray analysis of the natural aspartic proteinase inhibitor IA3 complexed with saccharopepsin from Saccharomyces cerevisiae

Acta Crystallogr D Biol Crystallogr. 2000 Jul;56(Pt 7):915-7. doi: 10.1107/s090744490000737x.

Abstract

The vacuolar aspartic proteinase from baker's yeast, saccharopepsin, has been co-crystallized with its natural inhibitor I(A)3, found in the cytosol. The I(A)3-saccharopepsin complex crystals belong to the space group P6(2)22, with unit-cell parameters a = b = 192.1, c = 59. 80 A and one molecule per asymmetric unit. The initial X-ray analysis of the complex indicates that the crystals diffract to 5.0 A, similar to native saccharopepsin crystals. This is probably a consequence in part of glycosylation of the native saccharopepsin. Full structural analysis of the complex crystal is in progress.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aspartic Acid Endopeptidases / chemistry*
  • Chromatography, High Pressure Liquid
  • Crystallization
  • Crystallography, X-Ray
  • Fungal Proteins / chemistry*
  • Fungal Proteins / isolation & purification*
  • Protein Conformation
  • Saccharomyces cerevisiae / enzymology*
  • Saccharomyces cerevisiae Proteins*

Substances

  • Fungal Proteins
  • PAI3 protein, S cerevisiae
  • Saccharomyces cerevisiae Proteins
  • aspartic proteinase A
  • Aspartic Acid Endopeptidases
  • YPS1 protein, S cerevisiae