Abstract
Alcohol oxidase fromPichia pastoris has been crystallized from polyethylene glycol 4000 solutions. The crystals are tetragonal, a=228 Å, c=456 Å space groupP41212. The crystals scatter only to about 6 Å 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 β/α-barrel (TIM barrel). This would indicate common ancestry with four other flavoenzymes: canavalin, glycolate oxidase, flavocytochrome b, and trimethylamine dehydrogenase.
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Tykarska, E., Lebioda, L., Marchut, E. et al. Crystallization of alcohol oxidase fromPichia pastoris. Secondary structure predictions indicate a domain with the eightfold β/α-barrel fold. J Protein Chem 9, 83–86 (1990). https://doi.org/10.1007/BF01024988
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DOI: https://doi.org/10.1007/BF01024988