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Structure of a unique twofold symmetric haem-binding site

Nature Structural Biology volume 1, pages 453–460 (1994)Cite this article

Abstract

Bacterioferritin of Escherichia coli, also known as cytochrome b1, is a hollow, nearly spherical shell made up of 24 identical protein subunits and 12 haems. We have solved this structure in a tetragonal crystal form at 2.9 Å resolution. We find that each haem is bound in a pocket formed by the interface between a pair of symmetry-related subunits. The quasi-twofold axis of the haem is closely aligned with the local twofold axis relating these subunits. The axial ligands of the haem are sulphurs of two equivalent methionyl residues (Met 52) from the symmetry-related subunits. A cluster of four water molecules is trapped in the gap between the upper edge of the haem and two extended protein loops which close off the haem from the outer aqueous environment. This is the first structure of a bis-methionine ligated haem-binding site and the first case of a twofold symmetric haem-binding site.

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Authors and Affiliations

  1. Department of Chemical Services, The Weizmann Institute of Science, Rehovot, 76100, Israel

    Felix Frolow

  2. Department of Structural Biology, The Weizmann Institute of Science, Rehovot, 76100, Israel

    A. Joseph Kalb (Gilboa)

  3. Laboratoire de Cristallographie et Physique Cristalline, Université de Bordeaux I, 33405, Talence, France

    Joseph Yariv

Authors
  1. Felix Frolow
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  2. A. Joseph Kalb (Gilboa)
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  3. Joseph Yariv
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Frolow, F., Kalb (Gilboa), A. & Yariv, J. Structure of a unique twofold symmetric haem-binding site. Nat Struct Mol Biol 1, 453–460 (1994). https://doi.org/10.1038/nsb0794-453

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