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The lipoamide arm in the glycine decarboxylase complex is not freely swinging

Nature Structural Biology volume 2, pages 63–68 (1995)Cite this article

Abstract

Glycine decarboxylase consists of four protein components. Its structural and mechanistic heart is provided by the lipoic acid-containing H-protein which undergoes a cycle of reductive methylamination, methylamine transfer and electron transfer. Lipoic acid attached to a specific lysine side chain is assumed to act as a ‘swinging arm’ conveying the reactive dithiolane ring from one catalytic centre to another. The X-ray crystal structures of two forms of the H-protein have been determined. The lipoate cofactor is located in the loop of a hairpin configuration but following methylamine transfer it is pivoted to bind into a cleft at the surface of the H-protein. The lipoamide-methylamine arm is, therefore, not free to move in aqueous solvent.

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Authors and Affiliations

  1. Institut de Biologie Structural, Centre National de la Recherche Scientifique et Commisariat à I'Energie Atomique, 41 av. des Martyrs, F38027, Grenoble Cedex, France

    Claudine Cohen-Addad & Serge Pares

  2. Department of Biological Structure, SM 20, University of Washington, Seattle, Washington, 98195, USA

    Larry Sieker

  3. Physiologie Cellulaire Végétale, Centre National de la Recherche Scientifique et Commisariat à I'Energie Atomique, Département de Biologie Moléculaire et Structural, 17 rue des Martyrs, F38054, Grenoble, Cedex 9, France

    Michel Neuburger & Roland Douce

Authors
  1. Claudine Cohen-Addad
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  2. Serge Pares
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  3. Larry Sieker
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  4. Michel Neuburger
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  5. Roland Douce
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Cohen-Addad, C., Pares, S., Sieker, L. et al. The lipoamide arm in the glycine decarboxylase complex is not freely swinging. Nat Struct Mol Biol 2, 63–68 (1995). https://doi.org/10.1038/nsb0195-63

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