Novel tetramer assembly of pyruvate decarboxylase from brewer's yeast observed in a new crystal form.
A new crystal form of thiamine diphosphate dependent pyruvate decarboxylase from Saccharomyces cerevisiae has been obtained in the presence of the activator pyruvamide. The crystallographic structure analysis reveals differences in the domain packing in the enzyme subunit and a novel assembly of the subunits in the tetramer, when compared to the structure of native PDC. The orientation of the beta domains in the subunit differs by a 6.3 degrees and 8.3 degrees rotation, respectively, whereas the subunit-subunit interface in the dimer, formed by the alpha and gamma domains, is essentially maintained. In the tetramer, one of the dimers rotates relative to the second dimer by approximately 30 degrees creating a new dimer-dimer interface.
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Department of Medical Biochemistry and Biophysics, Karolinska Institute, Stockholm, Sweden.
Dobritzsch
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König
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Schneider
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D003460:Crystallization; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D011487:Protein Conformation; D011767:Pyruvate Decarboxylase / Q000737:chemistry*; D011773:Pyruvates; D012441:Saccharomyces cerevisiae / Q000201:enzymology*
D011773:Pyruvates; D011767:Pyruvate Decarboxylase; C009144:pyruvamide