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3.2 Å structure of the copper-containing, oxygen-carrying protein Panulirus interruptus haemocyanin

Nature volume 309, pages 23–29 (1984)Cite this article

Abstract

For the first time, the three-dimensional structure of a member of the copper-containing class of oxygen-carrying proteins—the haemocyanins—has been determined. The structure of Panulirus interruptus haemocyanin at 3.2 Å resolution shows that each subunit of the 450,000-molecular weight hexamer is folded into three domains, and that the binuclear copper site is situated in the centre of the second domain. Amino acid sequence comparisons suggest that the polypeptide fold of P. interruptus haemocyanin is common to all arthropod haemocyanins.

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Authors and Affiliations

  1. Biomolecular Study Centre (BIOS), University of Groningen, Nijenborgh 16, 9747 AG, Groningen, The Netherlands

    W. P. J. Gaykema, W. G. J. Hol, J. M. Vereijken, N. M. Soeter, H. J. Bak & J. J. Beintema

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  1. W. P. J. Gaykema
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Gaykema, W., Hol, W., Vereijken, J. et al. 3.2 Å structure of the copper-containing, oxygen-carrying protein Panulirus interruptus haemocyanin. Nature 309, 23–29 (1984). https://doi.org/10.1038/309023a0

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