Preliminary crystallographic data for the thiamin diphosphate-dependent enzyme pyruvate decarboxylase from brewers' yeast

F. Dyda, W. Furey, S. Swaminathan, M. Sax, B. Farrenkopf, F. Jordan

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Abstract

Single crystals of the thiamin diphosphate (the vitamin B1 coenzyme)-dependent enzyme pyruvate decarboxylase (EC 4.1.1.1) from brewers' yeast have been grown using polyethylene glycol as a precipitating agent. Crystals of the homotetrameric version α4 of the holoenzyme are triclinic, space group P1, with cell constants a = 81.0, b = 82.4, c = 116.6 Å, α = 69.5, β = 72.6, γ = 62.4°. The crystals are reasonably stable in a rotating anode x-ray beam and diffract to at least 2.5 Å resolution. The V(m) value of 2.55 Å/dalton is consistent with a unit cell containing four subunits with mass of approximately 60 kDa each. Rotation function results with native data indicate strong noncrystallographic 222 symmetry relating the four identical subunits, thus density averaging methods are likely to play a role in the structure determination.

Original languageEnglish (US)
Pages (from-to)17413-17415
Number of pages3
JournalJournal of Biological Chemistry
Volume265
Issue number29
StatePublished - Nov 12 1990

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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