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<StructureSection load='1ecr' size='340' side='right'caption='[[1ecr]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
<StructureSection load='1ecr' size='340' side='right'caption='[[1ecr]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1ecr]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_(strain_b) Escherichia coli (strain b)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ECR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ECR FirstGlance]. <br>
<table><tr><td colspan='2'>[[1ecr]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_B Escherichia coli B]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ECR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ECR FirstGlance]. <br>
</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=1ecr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ecr OCA], [http://pdbe.org/1ecr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ecr RCSB], [http://www.ebi.ac.uk/pdbsum/1ecr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ecr ProSAT]</span></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]] 2.7&#8491;</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=1ecr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ecr OCA], [https://pdbe.org/1ecr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ecr RCSB], [https://www.ebi.ac.uk/pdbsum/1ecr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ecr ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[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=1ecr ConSurf].
</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=1ecr ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystal structure of the Escherichia coli replication-terminator protein (Tus) bound to terminus-site (Ter) DNA has been determined at 2.7 A resolution. The Tus protein folds into a previously undescribed architecture divided into two domains by a central basic cleft. This cleft accommodates locally deformed B-form Ter DNA and makes extensive contacts with the major groove, mainly through two interdomain beta-strands. The unusual structural features of this complex may explain how the replication fork is halted in only one direction.
Structure of a replication-terminator protein complexed with DNA.,Kamada K, Horiuchi T, Ohsumi K, Shimamoto N, Morikawa K Nature. 1996 Oct 17;383(6601):598-603. PMID:8857533<ref>PMID:8857533</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1ecr" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Replication Termination Protein|Replication Termination Protein]]
*[[Replication Termination Protein|Replication Termination Protein]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Escherichia coli B]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Kamada, K]]
[[Category: Kamada K]]
[[Category: Morikawa, K]]
[[Category: Morikawa K]]
[[Category: Dna replication]]
[[Category: Dna-binding]]
[[Category: Replication-dna complex]]
Retrieved from "https://proteopedia.org/1ecr"