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One-step evolution of a dimer from a monomeric protein

Nature Structural Biology volume 2, pages 746–751 (1995)Cite this article

Abstract

Deletion of six amino acids in a surface loop transforms staphylococcal nuclease from a monomeric protein into a very stable dimer (Kd<1×10−8M). A 2 Å X-ray crystal structure of the dimer (R=0.176) shows that the carboxy-terminal α-helix has been stripped from its normal position in one monomer and is now incorporated into the equivalent position on the adjoining monomer. This swapping creates an association interface of 2900 Å2. A second, smaller interface of 460 Å2 is also formed. The spontaneous exchange or swapping of secondary structural elements provides a simple pathway for the formation of large, stable protein/protein interfaces and may play an important role in the evolution of oligomeric proteins.

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Author notes

  1. Alan K. Meeker

    Present address: The Johns Hopkins University School of Medicine, 725 North Wolfe Street, Baltimore, Maryland, 21205, USA

Authors and Affiliations

  1. Department of Biophysics and Biophysical Chemistry, The Johns Hopkins University School of Medicine, 725 North Wolfe Street, Baltimore, Maryland, 21205, USA

    Susan M. Green, Apostolos G. Gittis & Eaton E. Lattman

  2. Department of Biological Chemistry, The Johns Hopkins University School of Medicine, 725 North Wolfe Street, Baltimore, Maryland, 21205, USA

    Alan K. Meeker

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  1. Susan M. Green
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  2. Apostolos G. Gittis
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  3. Alan K. Meeker
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  4. Eaton E. Lattman
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Green, S., Gittis, A., Meeker, A. et al. One-step evolution of a dimer from a monomeric protein. Nat Struct Mol Biol 2, 746–751 (1995). https://doi.org/10.1038/nsb0995-746

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