3mkw

<StructureSection load='3mkw' size='340' side='right' caption='[[3mkw]], [[Resolution|resolution]] 2.99&Aring;' scene=''>

<table><tr><td colspan='2'>[[3mkw]] 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=3MKW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MKW FirstGlance]. <br>

</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>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3mky|3mky]], [[3mkz|3mkz]]</td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">B, ECOK12F047, F plasmid, sopB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=3mkw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mkw OCA], [http://pdbe.org/3mkw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3mkw RCSB], [http://www.ebi.ac.uk/pdbsum/3mkw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3mkw ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/SOPB_ECOLI SOPB_ECOLI]] Control of plasmid partitioning; required to recognize the cis-acting. Binds specifically with the DNA segment containing the sopC region. SopB is trans-acting.

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== Publication Abstract from PubMed ==

Accurate DNA segregation is essential for genome transmission. Segregation of the prototypical F plasmid requires the centromere-binding protein SopB, the NTPase SopA and the sopC centromere. SopB displays an intriguing range of DNA-binding properties essential for partition; it binds sopC to form a partition complex, which recruits SopA, and it also coats DNA to prevent non-specific SopA-DNA interactions, which inhibits SopA polymerization. To understand the myriad functions of SopB, we determined a series of SopB-DNA crystal structures. SopB does not distort its DNA site and our data suggest that SopB-sopC forms an extended rather than wrapped partition complex with the SopA-interacting domains aligned on one face. SopB is a multidomain protein, which like P1 ParB contains an all-helical DNA-binding domain that is flexibly attached to a compact (beta(3)-alpha)(2) dimer-domain. Unlike P1 ParB, the SopB dimer-domain does not bind DNA. Moreover, SopB contains a unique secondary dimerization motif that bridges between DNA duplexes. Both specific and non-specific SopB-DNA bridging structures were observed. This DNA-linking function suggests a novel mechanism for in trans DNA spreading by SopB, explaining how it might mask DNA to prevent DNA-mediated inhibition of SopA polymerization.

Insight into F plasmid DNA segregation revealed by structures of SopB and SopB-DNA complexes.,Schumacher MA, Piro KM, Xu W Nucleic Acids Res. 2010 Jul;38(13):4514-26. Epub 2010 Mar 17. PMID:20236989<ref>PMID:20236989</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 3mkw" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Ecoli]]

[[Category: Piro, K]]

[[Category: Schumacher, M A]]

[[Category: Xu, W]]

[[Category: Centromere]]

[[Category: Dna binding protein-dna complex]]

[[Category: Sopb]]