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2Z9O

Crystal structure of the dimeric form of RepE in complex with the repE operator DNA

Summary for 2Z9O
Entry DOI10.2210/pdb2z9o/pdb
DescriptorDNA (33-MER), Replication initiation protein (3 entities in total)
Functional Keywordsreplication initiator, autogenous repressor, protein-dna complex, winged helix-turn-helix, dna replication, dna-binding, replication-dna complex, replication/dna
Biological sourceEscherichia coli
Total number of polymer chains4
Total formula weight82564.05
Authors
Nakamura, A.,Wada, C.,Miki, K. (deposition date: 2007-09-21, release date: 2007-11-27, Last modification date: 2023-11-01)
Primary citationNakamura, A.,Wada, C.,Miki, K.
Structural basis for regulation of bifunctional roles in replication initiator protein
Proc.Natl.Acad.Sci.Usa, 104:18484-18489, 2007
Cited by
PubMed 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 monomer, whereas the relative domain orientations are strikingly different, allowing for an efficient oligomeric transition of dual-functional RepE. This domain relocation accompanies secondary structural changes in the linker connecting the two domains, and the linker is included in plausible DnaK/DnaJ-binding regions. These findings suggest an activation mechanism for F plasmid replication by RepE monomerization, which is induced and mediated by the DnaK system.
PubMed: 18000058
DOI: 10.1073/pnas.0705623104
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.14 Å)
Structure validation

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