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The structure of the E. coli recA protein monomer and polymer

Nature volume 355, pages 318–325 (1992)Cite this article

An Erratum to this article was published on 06 February 1992

Abstract

The crystal structure of the recA protein from Escherichia coli at 2.3-Å resolution reveals a major domain that binds ADP and probably single- and double-stranded DNA. Two smaller subdomains at the N and C termini protrude from the protein and respectively stabilize a 61 helical polymer of protein subunits and interpolymer bundles. This polymer structure closely resembles that of recA/DNA filaments determined by electron microscopy. Mutations in recA protein that enhance coprotease, DNA-binding and/or strand-exchange activity can be explained if the interpolymer interactions in the crystal reflect a regulatory mechanism in vivo.

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Author notes

  1. Irene T. Weber

    Present address: Department of Pharmacology, Thomas Jefferson University, Philadelphia, Pennsylvania, 19107, USA

Authors and Affiliations

  1. Department of Molecular Biophysics and Biochemistry, and Department of Chemistry and Howard Hughes Medical Institute at Yale University, New Haven, Connecticut, 06511, USA

    Randall M. Story, Irene T. Weber & Thomas A. Steitz

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  1. Randall M. Story
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  2. Irene T. Weber
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Story, R., Weber, I. & Steitz, T. The structure of the E. coli recA protein monomer and polymer. Nature 355, 318–325 (1992). https://doi.org/10.1038/355318a0

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