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'''THE STRUCTURE OF THE E. COLI RECA PROTEIN MONOMER AND POLYMER''' | '''THE STRUCTURE OF THE E. COLI RECA PROTEIN MONOMER AND POLYMER''' | ||
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[[Category: Steitz, T A.]] | [[Category: Steitz, T A.]] | ||
[[Category: Story, R M.]] | [[Category: Story, R M.]] | ||
[[Category: | [[Category: Homologous recombination]] | ||
[[Category: | [[Category: Self-cleavage stimulation]] | ||
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Revision as of 16:44, 4 May 2008
THE STRUCTURE OF THE E. COLI RECA PROTEIN MONOMER AND POLYMER
OverviewOverview
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.
About this StructureAbout this Structure
2REB is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
The structure of the E. coli recA protein monomer and polymer., Story RM, Weber IT, Steitz TA, Nature. 1992 Jan 23;355(6358):318-25. PMID:1731246 Page seeded by OCA on Sun May 4 16:44:16 2008