Crystallization and preliminary crystallographic characterization of aspartic proteinase-A from baker's yeast and its complexes with inhibitors

J Mol Biol. 1993 Jul 20;232(2):701-3. doi: 10.1006/jmbi.1993.1420.

Abstract

The aspartic proteinase from yeast vacuoles, proteinase-A, has been crystallized with and without non-hydrolysable transition-state analogue inhibitors. The native enzyme crystals belong to the space group I2(1)2(1)2(1), with two molecules per asymmetric unit. The inhibitor complex crystals are trigonal with space group P3(2)21 and with one molecule in the asymmetric unit. Preliminary X-ray analysis of both native enzyme and its complexes indicate that the complexes diffract to higher resolution than the native crystals. This is probably due to reduced flexibility in the enzyme-inhibitor complex.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aspartic Acid Endopeptidases / antagonists & inhibitors*
  • Aspartic Acid Endopeptidases / chemistry*
  • Aspartic Acid Endopeptidases / metabolism
  • Chymosin / antagonists & inhibitors
  • Crystallization
  • Fungal Proteins / chemistry*
  • Fungal Proteins / metabolism
  • Oligopeptides / chemistry
  • Oligopeptides / metabolism
  • Organophosphorus Compounds / chemistry
  • Organophosphorus Compounds / metabolism
  • Saccharomyces cerevisiae / enzymology*
  • Saccharomyces cerevisiae Proteins
  • X-Ray Diffraction

Substances

  • Fungal Proteins
  • Oligopeptides
  • Organophosphorus Compounds
  • Saccharomyces cerevisiae Proteins
  • CP 81282
  • PD 130327
  • aspartic proteinase A
  • PEP4 protein, S cerevisiae
  • Aspartic Acid Endopeptidases
  • Chymosin