Structural basis for regulation of bifunctional roles in replication initiator protein.

ABSTRACT: DNA replication initiator protein RepE stringently regulates F plasmid replication by its two distinct molecular association states. A predominant dimer functions as an autogenous repressor, whereas monomers act as replication initiators, and the dimer requires actions of the DnaK molecular chaperone system for monomerization. The structure of the monomeric form is known, whereas the dimeric structure and structural details of the dimer-to-monomer conversion have been unclear. Here we present the crystal structure of the RepE dimer in complex with the repE operator DNA. The dimerization interface is mainly formed by intermolecular beta-sheets with several key interactions of charged residues. The conformations of the internal N- and C-terminal domains are conserved between the dimer and mo

SUBMITTER: Nakamura A 

PROVIDER: S-EPMC2141803 | biostudies-literature | 2007 Nov

REPOSITORIES: biostudies-literature