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Sequence and structure of D-glyceraldehyde 3-phosphate dehydrogenase from Bacillus stearothermophilus

Nature volume 266, pages 328–333 (1977)Cite this article

Abstract

The glyceraldehyde 3-phosphate dehydogenase holoenzyme of Bacillus stearothermophilus possesses precise 222 symmetry: in this respect it differs from the reported structure of the lobster muscle enzyme. Pairs of active sites are linked through a flexible polypeptide loop which probably mediates the structural changes giving rise to cooperative effects. Three additional salt bridges made by each subunit to others would make a major contribution to thermostability of the tetramer.

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Author notes

  1. G. Biesecker

    Present address: Scripps Clinic & Research Foundation, 476 Prospect Street, La Jolla, California, 92037

  2. J. C. Thierry

    Present address: Institut de Chimie, 1 Rue Blaise Pascal, 67008, Strasbourg Cedex, France

Authors and Affiliations

  1. MRC Laboratory of Molecular Biology, Hills Road, Cambridge, UK

    G. Biesecker, J. Ieuan Harris, J. C. Thierry, J. E. Walker & A. J. Wonacott

Authors
  1. G. Biesecker
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  2. J. Ieuan Harris
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  3. J. C. Thierry
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  4. J. E. Walker
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  5. A. J. Wonacott
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Biesecker, G., Ieuan Harris, J., Thierry, J. et al. Sequence and structure of D-glyceraldehyde 3-phosphate dehydrogenase from Bacillus stearothermophilus. Nature 266, 328–333 (1977). https://doi.org/10.1038/266328a0

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