2i05: Difference between revisions

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 <StructureSection load='2i05' size='340' side='right'caption='[[2i05]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2i05]] is a 3 chain structure with sequence from [https://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=2I05 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2I05 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2i05]] is a 3 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=2I05 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2I05 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene></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]] 2.6&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2io6|2io6]], [[2ewj|2ewj]], [[1ecr|1ecr]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tus ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=2i05 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i05 OCA], [https://pdbe.org/2i05 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2i05 RCSB], [https://www.ebi.ac.uk/pdbsum/2i05 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2i05 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/TUS_ECOLI TUS_ECOLI]] Trans-acting protein required for termination of DNA replication. Binds to DNA replication terminator sequences (terA to terF) to prevent the passage of replication forks. The termination efficiency will be affected by the affinity of this protein for the terminator sequence.
+[https://www.uniprot.org/uniprot/TUS_ECOLI TUS_ECOLI] Trans-acting protein required for termination of DNA replication. Binds to DNA replication terminator sequences (terA to terF) to prevent the passage of replication forks. The termination efficiency will be affected by the affinity of this protein for the terminator sequence.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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 </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2i05 ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-During chromosome synthesis in Escherichia coli, replication forks are blocked by Tus bound Ter sites on approach from one direction but not the other. To study the basis of this polarity, we measured the rates of dissociation of Tus from forked TerB oligonucleotides, such as would be produced by the replicative DnaB helicase at both the fork-blocking (nonpermissive) and permissive ends of the Ter site. Strand separation of a few nucleotides at the permissive end was sufficient to force rapid dissociation of Tus to allow fork progression. In contrast, strand separation extending to and including the strictly conserved G-C(6) base pair at the nonpermissive end led to formation of a stable locked complex. Lock formation specifically requires the cytosine residue, C(6). The crystal structure of the locked complex showed that C(6) moves 14 A from its normal position to bind in a cytosine-specific pocket on the surface of Tus.
-A molecular mousetrap determines polarity of termination of DNA replication in E. coli.,Mulcair MD, Schaeffer PM, Oakley AJ, Cross HF, Neylon C, Hill TM, Dixon NE Cell. 2006 Jun 30;125(7):1309-19. PMID:16814717<ref>PMID:16814717</ref>
+==See Also==
+*[[Replication Termination Protein|Replication Termination Protein]]
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 2i05" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Bacillus coli migula 1895]]
+[[Category: Escherichia coli]]
 [[Category: Large Structures]]
-[[Category: Dixon, N E]]
+[[Category: Dixon NE]]
-[[Category: Mulcair, M D]]
+[[Category: Mulcair MD]]
-[[Category: Oakley, A J]]
+[[Category: Oakley AJ]]
-[[Category: Schaeffer, P M]]
+[[Category: Schaeffer PM]]
-[[Category: Protein-dna complex]]
-[[Category: Replication-dna complex]]