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The structure of crystalline profilin–β-actin

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Abstract

The three-dimensional structure of bovine profilin–β-actin has been solved to 2.55 Å resolution by X-ray crystallography. There are several significant local changes in the structure of β-actin compared with α-actin as well as an overall 5° rotation between its two major domains. Actin molecules in the crystal are organized into ribbons through intermolecular contacts like those found in oligomeric protein assemblies. Profilin forms two extensive contacts with the actin ribbon, one of which appears to correspond to the solution contact in vitro.

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Authors and Affiliations

  1. Department of Chemistry, Henry H. Hoyt Laboratory, Princeton University, Princeton, New Jersey, 08544, USA

    Clarence E. Schutt, James C. Myslik, Michael D. Rozycki & Nalin C. W. Goonesekere

  2. Department of Zoological Cell Biology, WGI, Arrhenius Laboratories for Natural Sciences, Stockholm University, S-10691, Stockholm, Sweden

    Uno Lindberg

Authors
  1. Clarence E. Schutt
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  2. James C. Myslik
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  3. Michael D. Rozycki
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  4. Nalin C. W. Goonesekere
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  5. Uno Lindberg
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Schutt, C., Myslik, J., Rozycki, M. et al. The structure of crystalline profilin–β-actin. Nature 365, 810–816 (1993). https://doi.org/10.1038/365810a0

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