2z9o

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

spinqualitylabelsall models 2z9o, resolution 3.14Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2z9o is a 4 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.14Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function REPE1_ECOLI Replication initiator in the monomeric form, and autogenous repressor in the dimeric form. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Structural basis for regulation of bifunctional roles in replication initiator protein.,Nakamura A, Wada C, Miki K Proc Natl Acad Sci U S A. 2007 Nov 20;104(47):18484-9. Epub 2007 Nov 13. PMID:18000058 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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