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| | ==Crystal structure of the dimeric form of RepE in complex with the repE operator DNA== | | ==Crystal structure of the dimeric form of RepE in complex with the repE operator DNA== |
| - | <StructureSection load='2z9o' size='340' side='right' caption='[[2z9o]], [[Resolution|resolution]] 3.14Å' scene=''> | + | <StructureSection load='2z9o' size='340' side='right'caption='[[2z9o]], [[Resolution|resolution]] 3.14Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2z9o]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Z9O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2Z9O FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2z9o]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Z9O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Z9O FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">repE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.14Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2z9o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2z9o OCA], [http://pdbe.org/2z9o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2z9o RCSB], [http://www.ebi.ac.uk/pdbsum/2z9o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2z9o ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2z9o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2z9o OCA], [https://pdbe.org/2z9o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2z9o RCSB], [https://www.ebi.ac.uk/pdbsum/2z9o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2z9o ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/REPE1_ECOLI REPE1_ECOLI]] Replication initiator in the monomeric form, and autogenous repressor in the dimeric form. | + | [https://www.uniprot.org/uniprot/REPE1_ECOLI REPE1_ECOLI] Replication initiator in the monomeric form, and autogenous repressor in the dimeric form. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ecoli]] | + | [[Category: Escherichia coli K-12]] |
| - | [[Category: Miki, K]]
| + | [[Category: Large Structures]] |
| - | [[Category: Nakamura, A]]
| + | [[Category: Miki K]] |
| - | [[Category: Wada, C]]
| + | [[Category: Nakamura A]] |
| - | [[Category: Autogenous repressor]]
| + | [[Category: Wada C]] |
| - | [[Category: Dna replication]]
| + | |
| - | [[Category: Dna-binding]]
| + | |
| - | [[Category: Protein-dna complex]] | + | |
| - | [[Category: Replication initiator]] | + | |
| - | [[Category: Replication-dna complex]] | + | |
| - | [[Category: Winged helix-turn-helix]] | + | |
| Structural highlights
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Nakamura A, Wada C, Miki K. Structural basis for regulation of bifunctional roles in replication initiator protein. Proc Natl Acad Sci U S A. 2007 Nov 20;104(47):18484-9. Epub 2007 Nov 13. PMID:18000058
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