Purification, co-crystallization and preliminary X--ray analysis of the natural aspartic proteinase inhibitor IA3 complexed with saccharopepsin from Saccharomyces cerevisiae.
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.
Departments of Microbiology and Oral Science, University of Minnesota, 18-246 Moos Tower, 515 Delaware Street SE, Minneapolis, MN 55455, USA. mohammed@dcmir.med.umn.edu.
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Badasso
J A
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Read
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Dhanaraj
J B
JB
Cooper
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Wood
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Blundell
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Dreyer
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Winther
D016282:Aspartic Acid Endopeptidases / Q000737:chemistry*; D002851:Chromatography, High Pressure Liquid; D003460:Crystallization; D018360:Crystallography, X-Ray; D005656:Fungal Proteins / Q000737:chemistry* / Q000302:isolation & purification*; D011487:Protein Conformation; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D029701:Saccharomyces cerevisiae Proteins
D005656:Fungal Proteins; C018134:PAI3 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; C022325:aspartic proteinase A; D016282:Aspartic Acid Endopeptidases; C499266:YPS1 protein, S cerevisiae