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Molecular symmetry of human glyceraldehyde 3-phosphate dehydrogenase and its transformation during coenzyme binding

Authors
Journal
Journal of Molecular Biology
0022-2836
Publisher
Elsevier
Publication Date
Volume
69
Issue
3
Identifiers
DOI: 10.1016/0022-2836(72)90255-0
Disciplines
  • Biology

Abstract

Abstract The objects of investigations were single crystals of glyceraldehyde 3-phosphate dehydrogenase. Precession X-ray diffraction patterns of several reciprocal lattice planes were obtained. The specifity of the molecular packing in crystals provided a direct possibility to find tetrahedral symmetry of a holo-enzyme molecule, while the decrease of the crystal symmetry during conversion from holo- to apo-form suggests the decrease of glyceraldehyde 3-phosphate dehydrogenase molecular symmetry during this process. This result is of interest in connection with the symmetry transformations of other dehydrogenases during NAD binding.

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