title: The structure of the E. coli recA protein monomer and polymer.
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.
authors.affiliation: Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06511.
authors.forename: R M
authors.initials: RM
authors.lastname: Story
authors.forename: I T
authors.initials: IT
authors.lastname: Weber
authors.forename: T A
authors.initials: TA
authors.lastname: Steitz
mesh_terms: 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
chemical_list: D004269:DNA, Bacterial; D046911:Macromolecular Substances; D011938:Rec A Recombinases