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3vw4

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==Crystal structure of the DNA-binding domain of ColE2-P9 Rep in complex with the replication origin==
==Crystal structure of the DNA-binding domain of ColE2-P9 Rep in complex with the replication origin==
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<StructureSection load='3vw4' size='340' side='right' caption='[[3vw4]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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<StructureSection load='3vw4' size='340' side='right'caption='[[3vw4]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3vw4]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VW4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VW4 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3vw4]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VW4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VW4 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rep ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<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=3vw4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vw4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vw4 RCSB], [http://www.ebi.ac.uk/pdbsum/3vw4 PDBsum]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3vw4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vw4 OCA], [https://pdbe.org/3vw4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vw4 RCSB], [https://www.ebi.ac.uk/pdbsum/3vw4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vw4 ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q06B24_ECOLX Q06B24_ECOLX]
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Duplex DNA is generally unwound by protein oligomers prior to replication. The Rep protein of plasmid ColE2-P9 (34 kDa) is an essential initiator for plasmid DNA replication. This protein binds the replication origin (Ori) in a sequence specific manner as a monomer and unwinds DNA. Here we present the crystal structure of the DNA-binding domain of Rep (E2Rep-DBD) in complex with Ori DNA. The structure unveils the basis for Ori specific recognition by the E2Rep-DBD and also reveals that it unwinds DNA by the concerted actions of its three contiguous structural modules. The structure also shows that the functionally unknown PriCT domain, which forms a compact module, plays a central role in DNA unwinding. The conservation of the PriCT domain in the C-termini of some archaeo-eukaryotic primases, indicates that it likely plays a similar role in these proteins. Thus, this is the first report providing the structural basis for the functional importance of the conserved PriCT domain and also reveals a novel mechanism for DNA unwinding by a single protein.
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Structural Basis for Replication Origin Unwinding by An Initiator-Primase of Plasmid ColE2-P9: Duplex DNA Unwinding by A Single Protein.,Itou H, Yagura M, Shirakihara Y, Itoh T J Biol Chem. 2014 Dec 23. pii: jbc.M114.595645. PMID:25538245<ref>PMID:25538245</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bacillus coli migula 1895]]
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[[Category: Escherichia coli]]
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[[Category: Itoh, T]]
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[[Category: Large Structures]]
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[[Category: Itou, H]]
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[[Category: Itoh T]]
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[[Category: Shirakihara, Y]]
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[[Category: Itou H]]
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[[Category: Yagura, M]]
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[[Category: Shirakihara Y]]
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[[Category: Cytosol]]
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[[Category: Yagura M]]
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[[Category: Dna binding protein-dna complex]]
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[[Category: Helix-turn-helix]]
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[[Category: Replication initiator protein]]
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[[Category: Specific dna-binding and unwinding of dna duplex]]
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Current revision

Crystal structure of the DNA-binding domain of ColE2-P9 Rep in complex with the replication origin

PDB ID 3vw4

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