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Nature. 1992 Jan 23;355(6358):318-25.

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

Author information

1
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06511.

Erratum in

  • Nature 1992 Feb 6;355(6360):567.

Abstract

The crystal structure of the recA protein from Escherichia coli at 2.3-A 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 6(1) 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.

PMID:
1731246
DOI:
10.1038/355318a0
[Indexed for MEDLINE]

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