Crystallization and initial X-ray diffraction analysis of human pyruvate dehydrogenase.
Human pyruvate dehydrogenase (E1) is a component enzyme of the pyruvate dehydrogenase complex. The enzyme catalyzes the irreversible decarboxylation of pyruvic acid and the rate-limiting reductive acetylation of the lipoyl moiety linked to the dihydrolipoamide acetyltransferase component of the pyruvate dehydrogenase complex. E1 is an alpha(2)beta(2) tetramer ( approximately 154 kDa). Crystals of this recombinant enzyme have been grown in polyethylene glycol 3350 using a vapor-diffusion method at 295 K. The crystals are characterized as orthorhombic, space group P2(1)2(1)2(1), with unit-cell parameters a = 64.2, b = 126.9, c = 190.2 A. Crystals diffracted to a minimum d spacing of 2.5 A. The asymmetric unit contains one alpha(2)beta(2) tetrameric E1 assembly; self-rotation function analysis showed a pseudo-twofold symmetry relating the two alphabeta dimers.
Universities Space Research Association, 4950 Corporate Drive, Huntsville, AL 35803, USA. ewa.ciszak@msfc.nasa.gov
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Ciszak
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Korotchkina
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Hong
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Joachimiak
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Patel
D003460:Crystallization; D018360:Crystallography, X-Ray; D006801:Humans; D011487:Protein Conformation; D011768:Pyruvate Dehydrogenase Complex / Q000737:chemistry*
D011768:Pyruvate Dehydrogenase Complex