Crystallization of alcohol oxidase from Pichia pastoris. Secondary structure predictions indicate a domain with the eightfold beta/alpha-barrel fold.
Alcohol oxidase from Pichia pastoris has been crystallized from polyethylene glycol 4000 solutions. The crystals are tetragonal, a = 228 A, c = 456 A space group P4(1)2(1)2. The crystals scatter only to about 6 A resolution; their poor crystallinity may have some physiological function. Secondary structure predictions suggest that the C-terminal part of the molecule, residues 311-664, has the folding of an eightfold beta/alpha-barrel (TIM barrel). This would indicate common ancestry with four other flavoenzymes: canavalin, glycolate oxidase, flavocytochrome b, and trimethylamine dehydrogenase.
Tykarska
E
E
Department of Chemistry, University of South Carolina, Columbia 29208.
Lebioda
L
L
Marchut
E
E
Steczko
J
J
Stec
B
B
D000429:Alcohol Oxidoreductases; D000595:Amino Acid Sequence; D003460:Crystallization; D008969:Molecular Sequence Data; D010843:Pichia / Q000201:enzymology*; D011487:Protein Conformation; D004718:Saccharomycetales / Q000201:enzymology*; D014961:X-Ray Diffraction
D000429:Alcohol Oxidoreductases; C019643:alcohol oxidase