2Z9O

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

2Z9O の概要

• エントリーDOI: 10.2210/pdb2z9o/pdb
• 分子名称: DNA (33-MER), Replication initiation protein (3 entities in total)
• 機能のキーワード: replication initiator, autogenous repressor, protein-dna complex, winged helix-turn-helix, dna replication, dna-binding, replication-dna complex, replication/dna
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 82564.05

構造登録者

Nakamura, A.,Wada, C.,Miki, K. (登録日: 2007-09-21, 公開日: 2007-11-27, 最終更新日: 2023-11-01)

主引用文献

Nakamura, 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

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

実験手法

X-RAY DIFFRACTION (3.14 Å)