The structure of the E. coli recA protein monomer and polymer.
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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Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06511.
Weber
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Steitz
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D000595:Amino Acid Sequence; D001665:Binding Sites; D004269:DNA, Bacterial / Q000378:metabolism; D004926:Escherichia coli / Q000378:metabolism*; D046911:Macromolecular Substances; D008958:Models, Molecular; D011487:Protein Conformation; D011938:Rec A Recombinases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D014961:X-Ray Diffraction / Q000379:methods
D004269:DNA, Bacterial; D046911:Macromolecular Substances; D011938:Rec A Recombinases