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T and R states in the crystals of bacterial L–lactate dehydrogenase reveal the mechanism for allosteric control

Nature Structural Biology volume 1, pages 176–185 (1994)Cite this article

Abstract

The crystal structure of L–lactate dehydrogenase from Bifidobacterium longum, determined to 2.5 Å resolution, contains a regular 1:1 complex of T– and R–state tetramers. A comparison of these two structures within the same crystal lattice and kinetical characterization of the T–R transition in solution provide an explanation for the molecular mechanism of allosteric activation. Substrate affinity is controlled by helix sliding between subunits which is triggered by the binding of the activator, fructose 1,6–bisphosphate. The proposed mechanism can explain activation by chemical modification and mutagenesis, as well as suggesting why vertebrate counterparts are not allosteric.

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Author notes

  1. So Iwata

    Present address: Max-Planck-lnstitut für Biophysik, Abteilung Molekulare Membranbiologie, Heinrich-Hoffmann-Straβe 7, 60528, Frankfurt am Main, Germany

Authors and Affiliations

  1. Department of Agricultural Chemistry, The University of Tokyo, Bunkyo-ku, Tokyo, 113, Japan

    So Iwata, Kenji Kamata, Sumiko Yoshida, Takashi Minowa & Takahisa Ohta

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  4. Takashi Minowa
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Iwata, S., Kamata, K., Yoshida, S. et al. T and R states in the crystals of bacterial L–lactate dehydrogenase reveal the mechanism for allosteric control. Nat Struct Mol Biol 1, 176–185 (1994). https://doi.org/10.1038/nsb0394-176

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