The structure of the E. coli recA protein monomer and polymer - PubMed (original) (raw)

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

doi: 10.1038/355318a0.

Affiliations

• PMID: 1731246
• DOI: 10.1038/355318a0

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

R M Story et al. Nature. 1992.

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.

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Comment in

• Molecular biology. recA: from locus to lattice.
  McEntee K. McEntee K. Nature. 1992 Jan 23;355(6358):302-3. doi: 10.1038/355302a0. Nature. 1992. PMID: 1731243 No abstract available.

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