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Structure of trimeric haemerythrin

Nature volume 303, pages 86–88 (1983)Cite this article

Abstract

Several simplifying structural principles have been developed from the considerable data contained in the three-dimensional structures of proteins determined in the past two decades. One of these is based on the observation that particular folding motifs often occur in a variety of structural and functional settings1. The compact bundle of four antiparallel α-helices2, first seen in the structure of myohaemerythrin3, is an example. Several non-haemerythrin proteins have since been found to have the same folding pattern4–7, and haemerythrins themselves exist in a wide variety of quaternary arrangements8,9. The unusual ability of the haemerythrin fold to associate as dimers, trimers, tetramers, octamers or higher aggregates provides an opportunity for examining structural diversity in subunit association. We have used X-ray crystallography to study the subunit structure of trimeric haemerythrin from a Siphonosoma species. We report here that the pattern of intersubunit helix–helix interactions differs from the most common mode of association of other helix-bundle proteins. In a novel approach to structure analysis at low resolution, experimental phases for the structure determination were based on anomalous scattering from the iron atoms native to haemerythrin, using the new resolved-anomalous phasing procedure10.

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Authors and Affiliations

  1. Laboratory for the Structure of Matter, Naval Research Laboratory 6030, Washington, DC, 20375, USA

    Janet L. Smith & Wayne A. Hendrickson

  2. Department of Chemistry, Drexel University, Philadelphia, Pennsylvania, 19104, USA

    Anthony W. Addison

Authors
  1. Janet L. Smith
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  2. Wayne A. Hendrickson
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  3. Anthony W. Addison
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Smith, J., Hendrickson, W. & Addison, A. Structure of trimeric haemerythrin. Nature 303, 86–88 (1983). https://doi.org/10.1038/303086a0

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