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The allosteric ligand site in the Vmax-type cooperative enzyme phosphoglycerate dehydrogenase

Nature Structural Biology volume 2, pages 69–76 (1995)Cite this article

Abstract

The crystal structure of the phosphoglycerate dehydrogenase from Eschehchia coli is unique among dehydrogenases. It consists of three clearly separate domains connected by flexible hinges. The tetramer has approximate 222 symmetry with the principal contacts between the subunits forming between either the nucleotide binding domains or the regulatory domains. Two slightly different subunit conformations are present which vary only in the orientations of the domains. There is a hinge-like arrangement near the active site cleft and the serine effector site is provided by the regulatory domain of each of two subunits. Interdomain flexibility may play a key role in both catalysis and allosteric inhibition.

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Authors and Affiliations

  1. Department of Molecular Biology, University of Califomia, Irvine, California, 92717, USA

    David J. Schuller

  2. Department of Molecular Biology and Pharmacology, and Department of Medicine, Washington University School of Medicine, St. Louis, Missouri, 63110, USA

    Gregory A. Grant

  3. Department of Biochemistry, University of Minnesota, Minneapolis, Minnesota, 55455, USA

    Leonard J. Banaszak

Authors
  1. David J. Schuller
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  2. Gregory A. Grant
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  3. Leonard J. Banaszak
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Schuller, D., Grant, G. & Banaszak, L. The allosteric ligand site in the Vmax-type cooperative enzyme phosphoglycerate dehydrogenase. Nat Struct Mol Biol 2, 69–76 (1995). https://doi.org/10.1038/nsb0195-69

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