Crystallization and preliminary X-ray analysis of carboxypeptidase Y inhibitor IC complexed with the cognate proteinase.
Carboxypeptidase Y (CPY) inhibitor I(C) is a naturally occurring serine carboxypeptidase inhibitor from Saccharomyces cerevisiae, the sequence of which is not homologous with any other known proteinase inhibitor and is classified as the phosphatidylethanolamine-binding protein (PEBP). I(C) has been crystallized in complex with the deglycosylated form of CPY by the hanging-drop vapour-diffusion technique with ammonium sulfate as a precipitant. The crystals of the complex belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 81.13, b = 186.6, c = 65.14 A. Diffraction data were collected to 2.7 A resolution. Structure determination of the complex is in progress by the molecular-replacement method using the structure of CPY as a search model.
Mima
Joji
J
Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan.
Hayashida
Minoru
M
Fujii
Tomomi
T
Hata
Yasuo
Y
Hayashi
Rikimaru
R
Ueda
Mitsuyoshi
M
D000645:Ammonium Sulfate / Q000737:chemistry; D002352:Carrier Proteins / Q000737:chemistry*; D002850:Chromatography, Gel; D003460:Crystallization; D018360:Crystallography, X-Ray; D003593:Cytoplasm / Q000737:chemistry; D004591:Electrophoresis, Polyacrylamide Gel; D006863:Hydrogen-Ion Concentration; D010714:Phosphatidylethanolamines / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry*
D002352:Carrier Proteins; D010714:Phosphatidylethanolamines; D029701:Saccharomyces cerevisiae Proteins; C496670:carboxypeptidase Y inhibitor IC, S cerevisiae; D000645:Ammonium Sulfate