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Cooperative dimeric and tetrameric clam haemoglobins are novel assemblages of myoglobin folds

Nature volume 316, pages 277–280 (1985)Cite this article

Abstract

Cooperative functioning of many protein systems depends on communication between different subunits of those systems. Perhaps the best understood cooperative protein system is the vertebrate haemoglobin tetramer, in which the subunits share a similar tertiary structure (the myoglobin fold) with each other and with myoglobins and haemoglobins from at least four different animal phyla and leguminous plants. Blood clams have cooperative tetrameric haemoglobin and, in addition, a cooperative homodimeric haemoglobin 1–6. In view of previous reports7,8 concerning the role of dimers in the vertebrate tetramer, the clam haemoglobins represent a very interesting model system. We report here the low-resolution three-dimensional crystal structures of the dimeric and turmeric cooperative hemoglobins from the blood clam Scapharca inaequivalvis. We find that clam haemoglobins are made of myoglobin-like subunits but their assembly to form dimers and tetramers is quite different from that of vertebrate haemoglobin. The arrangement of the subunits provides a simple structural explanation for haem-haem interaction in the dimer and tetramer.

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Author notes

  1. William E. Royer Jr

    Present address: Department of Biochemistry and Molecular Biophysics, Columbia University, 630 W. 168th Street, New York, New York, 10032, USA

  2. Faith F. Fenderson

    Present address: Department of Biochemistry, University of Washington, Seattle, Washington, 98195, USA

Authors and Affiliations

  1. Thomas C. Jenkins Department of Biophysics, Johns Hopkins University, 3400 N. Charles Street, Baltimore, Maryland, 21218, USA

    William E. Royer Jr, Warner E. Love & Faith F. Fenderson

Authors
  1. William E. Royer Jr
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  2. Warner E. Love
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  3. Faith F. Fenderson
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Royer, W., Love, W. & Fenderson, F. Cooperative dimeric and tetrameric clam haemoglobins are novel assemblages of myoglobin folds. Nature 316, 277–280 (1985). https://doi.org/10.1038/316277a0

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