2.8-angstrom structure of yeast serine carboxypeptidase

Multiple isomorphous replacement and crystallographic refinement at 2.8 Angstroms help determine the crystal structure of monomeric yeast serine carboxypeptidase (CPD-Y) isolated from Saccharomyces cerevisiae. A comparative study of the structures of S. cerevisiae CPD-Y and wheat serine CPD-Y helps examine the molecular basis for different substrate specificities. The difference is due to replacement of negatively charged residues in wheat serine CPD by hydrophobic residues in CPD-Y.