Crystallization of inhibited aspartic proteinase from Candida albicans.
A major secreted aspartic proteinase from Candida albicans has been crystallized in the presence of inhibitors to prevent autodegradation. With pepstatin a cleaved form of the enzyme was nevertheless found in the crystals whereas with the inhibitor A70450 the enzyme remained intact. The crystals containing pepstatin were not suitable for X-ray data collection while the crystals containing A70450 grew by vapour diffusion as tetragonal bipyramids, space group P4(3)2(1)2 (or P4(1)2(1)2), a = b = 76.2 A, c = 126.1 A, with one molecule in the asymmetric unit and they diffract to beyond 2.2 A.
Cutfield
S
S
Biochemistry Department, University of Otago, Dunedin, New Zealand.
Marshall
C
C
Moody
P
P
Sullivan
P
P
Cutfield
J
J
D016282:Aspartic Acid Endopeptidases / Q000037:antagonists & inhibitors* / Q000737:chemistry / Q000648:ultrastructure; D002176:Candida albicans / Q000201:enzymology*; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D010436:Pepstatins / Q000737:chemistry; D010879:Piperazines / Q000737:chemistry; D017434:Protein Structure, Tertiary
D010436:Pepstatins; D010879:Piperazines; C014195:Streptomyces pepsin inhibitor; C083088:A 70450; D016282:Aspartic Acid Endopeptidases; C031375:pepstatin