The structure of the E. coli recA protein monomer and polymer. |
| |
Authors: | R M Story I T Weber T A Steitz |
| |
Affiliation: | Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06511. |
| |
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. |
| |
Keywords: | |
|
|